Transcription Factors

Transcription is the process of creating a complementary RNA copy of a sequence of DNA. The result of transcription is messenger RNA (mRNA), which will then be used to create a protein via the process of translation.
Transcription factors are essential for the control of gene expression. These molecules bind to specific DNA sequences, controlling the transcription of genetic information from DNA to mRNA. Transcription factors can activate or repress transcription to regulate gene expression. As such, they are vital for many important cellular processes. Sigma-Aldrich has a large selection of products to aid research on the mechanisms of DNA-RNA transcription.

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SRP0312 AEBP2 human recombinant, expressed in baculovirus infected Sf9 cells, ≥48% (SDS-PAGE)  
SML0009 AI-1 ≥98% (HPLC) AI-1 promotes Nrf2 activation via the covalent modification of Kelch-like ECH-associated protein 1 (Keap1), a negative regulator of Nrf2. Biochemical studies indicate that an aromatic chloride present within the AI-1 molecule undergoes a nucleophilic aromatic substitution reaction with cysteine thiols of Keap1.
SRP2103 Arginine Splicing Factor, His tagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) ASF or called SF2, a member of the SR protein family, is an essential pre-mRNA splicing factor required for both single and alternative splicing. Phosphorylation on serine residues located within the SR domain directly regulates ASF/SF2 activity and compartmentalization of other SR splicing factors. In addition to interacting with RNA and other splicing factors, such as U1-70K, U2AF and other SR proteins, ASF/SF2 also directly or indirectly interacts with HIV regulatory protein Rev, the C-terminal domain (CTD) of the largest subunit of RNA polymerase II, and numerous transcription factors, thereby suggesting a potential role of ASF/SF2 in coordinating of transcription and pre-mRNA splicing.
SRP2104 Arginine Splicing Factor, His tagged human recombinant, expressed in insect cells, ≥85% (SDS-PAGE) ASF also known as SF2 is a member of the SR protein family. It is an essential pre-mRNA splicing factor required for both single and alternative splicing. Phosphorylation on serine residues located within the SR domain directly regulates ASF/SF2 activity and compartmentalization of other SR splicing factors. In addition to interacting with RNA and other splicing factors, such as U1-70K, U2AF and other SR proteins, ASF/SF2 also directly or indirectly interacts with HIV regulatory protein Rev, the C-terminal domain (CTD) of the largest subunit of RNA polymerase II, and numerous transcription factors, thereby suggesting a potential role of ASF/SF2 in coordinating transcription and pre-mRNA splicing.
A2353 ATF-2 human ≥90% (SDS-PAGE), recombinant, expressed in E. coli, N-terminal maltose binding protein tagged, lyophilized powder  
SRP5163 ATF1, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP2149 ATF2 (19-96), GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE) The activating transcription factor 2 (ATF2), known as CRE-BP1 (cAMP-responsive element binding protein 1), is a member of the leucine zipper family of DNA binding proteins and binds to both AP-1 and CRE DNA response elements of many viral and cellular promoters. ATF2 is activated by diverse cellular stresses such as inflammatory cytokines, genotoxic agents and UV irradiation. It is activated through phosphorylation at two phospho sites of Thr69 and Thr71 by upstream activators like JNK/p38 (MAPK14, SAPK2A). GST-ATF2 [19-96] is preferentially used as a useful substrate for MAPK14 and was assayed using MAPK14 by luminescence-based ATP depletion assay.
SRP2080 BRCA1 human recombinant, expressed in insect cells, ≥70% (SDS-PAGE) The human BRCA1, the product of breast and ovarian cancer gene 1, is a hyperphosphorylated protein functioning as a tumor suppressor involved in both transcription regulation and DNA repair. BRCA1 associates with RAD51 and has shown to be required for transcription-coupled repair of DNA damage as well as for the repair of chromosomal double-strand breaks. Association with a human SWI/SNF-related complex has recently suggested a potential role of BRCA1 in linking chromatin remodeling to breast cancer.
SRP0449 BRD1 (561-668) GST tag human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)  
SRP0448 BRD1 (561-668) His tag human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)  
SRP0451 BRD2 (65-187) GST tag human recombinant, expressed in E. coli, ≥81% (SDS-PAGE)  
SRP0452 BRD2 (65-187) His tag human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)  
SRP0453 BRD2 (339-459) GST tag human recombinant, expressed in E. coli, ≥86% (SDS-PAGE)  
SRP0450 BRD2 (339-459) His tag human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)  
SRP0454 BRD2, BD1, BD2 (65-459) GST tag human recombinant, expressed in E. coli, ≥80% (SDS-PAGE)  
SRP0457 BRD3 (29-145) GST tag human recombinant, expressed in E. coli, ≥81% (SDS-PAGE)  
SRP0455 BRD3 (29-145) His tag human recombinant, expressed in E. coli, ≥88% (SDS-PAGE)  
SRP0458 BRD3 (306-417) GST tag human recombinant, expressed in E. coli, ≥82% (SDS-PAGE)  
SRP0456 BRD3 (306-417) His tag human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)  
SRP0459 BRD4 (49-170) GST tag human recombinant, expressed in E. coli, ≥82% (SDS-PAGE) BRD4 (bromodomain-containing protein 4) works as a reader of epigenetic marks and is involved in chromatin remodeling and transcriptional regulation. Therefore, it is a target for oncology, inflammation and cardiovascular disease. This gene is upregulated in hepatocellular carcinoma and is associated with poor prognosis. BRD4 is also associated with melanoma, hepatocellular carcinoma, multiple myeloma, Burkitt′s lymphoma, acute myeloid leukemia and breast cancer. BRD4 connects cell cycle and transcription, works as a scaffold for transcription factors and bookmarks active genes during mitosis. It interacts with acetylated histone-3 and histone-4 tails and helps in maintaining chromatin architecture. Also, it regulates transcription elongation via phosphorylation of RNA polymerase II.
SRP0461 BRD4 (49-170) His tag human recombinant, expressed in E. coli, ≥90% (SDS-PAGE) BRD4 (bromodomain-containing protein 4) works as a reader of epigenetic marks and is involved in chromatin remodeling and transcriptional regulation. Therefore, it is a target for oncology, inflammation and cardiovascular disease. This gene is upregulated in hepatocellular carcinoma and is associated with poor prognosis. BRD4 is also associated with melanoma, hepatocellular carcinoma, multiple myeloma, Burkitt′s lymphoma, acute myeloid leukemia and breast cancer. BRD4 connects cell cycle and transcription, works as a scaffold for transcription factors and bookmarks active genes during mitosis. It interacts with acetylated histone-3 and histone-4 tails and helps in maintaining chromatin architecture. Also, it regulates transcription elongation via phosphorylation of RNA polymerase II.
SRP0460 BRD4 (342-460) GST tag human recombinant, expressed in E. coli, ≥75% (SDS-PAGE)  
SRP0462 BRD4 (342-460) His tag human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)  
SRP0463 BRD4, BD1, BD2 (49-460) GST tag human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) BRD4 (bromodomain-containing protein 4) works as a reader of epigenetic marks and is involved in chromatin remodeling and transcriptional regulation. Therefore, it is a target for oncology, inflammation and cardiovascular disease. This gene is upregulated in hepatocellular carcinoma and is associated with poor prognosis. BRD4 is also associated with melanoma, hepatocellular carcinoma, multiple myeloma, Burkitt′s lymphoma, acute myeloid leukemia and breast cancer. BRD4 connects cell cycle and transcription, works as a scaffold for transcription factors and bookmarks active genes during mitosis. It interacts with acetylated histone-3 and histone-4 tails and helps in maintaining chromatin architecture. Also, it regulates transcription elongation via phosphorylation of RNA polymerase II.
SRP0464 BRD4, BD1, BD2 (49-460) His tag human recombinant, expressed in E. coli, ≥75% (SDS-PAGE)  
SRP0473 BRDT (22-138) GST tag human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)  
SRP0466 BRDT (22-138) His tag human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)  
SRP0465 BRDT (257-382) His tag human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)  
SRP0467 BRG1 (1480-1603) His tag human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)  
SRP2037 BRG1-mt, K798R human recombinant, expressed in insect cells, ≥80% (SDS-PAGE) BRG1 is an essential component of the SWI/SNF chromatin remodeling complexes and is implicated in multiple functions through its interaction with different proteins, including the tumor suppressor protein pRb, serine-threonine kinase LKB1, and other transcription factors. Mutation of lysine to arginine at position 798 in the DNA-dependent ATPase domain of BRG1 a) failed to restore normal growth to swi2- cells, b) reduced its ability to repress c-fos transcription, and c) reduced CIITA (class II transactivator) induction and enhanced the rate of induction of the interferon-g-responsive GBP-1 gene.
SRP2036 BRG1, wild type human recombinant, expressed in insect cells, ≥80% (SDS-PAGE) The wild type human brahma-related gene 1 (Brg1) encodes a protein of 1,647 amino acids that contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription regulation. BRG1 is an essential component of the SWI/SNF chromatin remodeling complexes and implicated in multiple functions through its interaction with different proteins, including the tumor suppressor protein pRb, serine-threonine kinase LKB1, and other transcription factors. Although Brg1 is involved in chromatin remodeling as a complex with other SWI/SNF proteins, purified BRG1 itself is capable of remodeling mono-nucleosomes and nucleosomal arrays in vitro. Mutations of Brg1 have been found in multiple tumor cell lines.
SRP2067 CAR, ligand binding domain (101-348) human recombinant, expressed in E. coli, ≥85% (SDS-PAGE) The constitutive androstane receptor (CAR) was identified as a member of the orphan nuclear hormone receptor family in 1994. Although constitutively active, it can be further activated by `phenobarbitol-like` compounds, the most potent being the synthetic compound TCPOBOP. Upon activation, CAR regulates the xenobiotic drug metabolizing enzymes, cytochrome P450s. There are several overlapping functions between the nuclear receptors PXR and CAR. Recently, CAR, as well as PXR, have been shown to place a role in bile acid clearance and cholestatic liver injury.
SRP5173 CBP (1319-1710), GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution CBP or CREB-binding protein is a nuclear transcriptional coactivator protein that binds specifically to the PKA-phosphorylated form of the CREB protein. Microinjection of an anti-CBP antiserum into fibroblasts leads to inhibition of transcription from a cAMP promoter. CBP can also cooperates with upstream activators, such as JUN. When JUN is phosphorylated at the transcriptionally stimulatory sites ser73 and ser63, it binds CBP with comparable affinity to CREB. Insulin signaling may directly regulate many cAMP signaling pathways at the transcriptional level by controlling CBP recruitment. Mutant CBP can be aberrantly recruited to CREB protein, resulting in inappropriate activation of gluconeogenesis and glucose intolerance.
SRP5177 CREB1 (1-280), GST tagged from rat recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP0483 CREBBP (1081-1197) His tag human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)  
SRP2031 CTF1 human recombinant, expressed in insect cells, ≥70% (SDS-PAGE) The CCAAT-box binding protein 1 (CTF1, also called NF-I or NF-1) is a proline-rich transcription activator. It selectively activates transcription of genes that contain GCCAAT consensus sequence in promoter region, including human Ha-Ras, alpha-globin, hsp70 and many other cellular and viral genes. Cloning and functional characterization of the protein revealed that CTF1 contains an N-terminal DNA binding domain and a C-terminal proline-rich activation domain. CTF1 was shown to interact with the general transcription factor IIB (TFIIB) and facilitate the recruitment of TFIIB to TBP-DNA complexes, with the forkhead thyroid transcription factor TTF2 to regulate hormone–dependent transcription of thyroperoxidase gene, as well as other receptor proteins to synergize hormone receptor-responsive activation.
SRP2122 CTF1, GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE) The CCAAT-box binding protein 1 (CTF1, also called NF-I or NF-1) is a proline-rich transcription activator. It selectively activates transcription of genes that contain GCCAAT consensus sequence in the promoter region, including human Ha-Ras, alpha-globin, hsp70 and many other cellular and viral genes. Cloning and functional characterization of the protein revealed that CTF1 contains a N-terminal DNA binding domain and a C-terminal proline-rich activation domain. CTF1 was shown to interact with the general transcription factor IIB (TFIIB) and facilitate the recruitment of TFIIB to TBP-DNA complexes, with the forkhead thyroid transcription factor TTF2 to regulate hormone-dependent transcription of thyroperoxidase gene, as well as other receptor proteins to synergize hormone receptor-responsive activation.
SRP2021 Dr1 (NC2b, 19 kDa) human recombinant, expressed in E. coli, ≥70% (SDS-PAGE) Dr1 is a general negative regulator of class II and class III gene expression. It binds to the basic repeat domain of TBP on promoter DNA and can prevent the RNA polymerase II holoenzyme, or its TFIIB and/or TFIIA subunits, from assembling into an initiation complex. Dr1 is phosphorylated in vivo and this modification affects its interaction with TBP. In addition, Dr1 interacts with the hyperphosphorylated form of Pol II and with the repression domain of the AREB6 repressor. Dr1 forms a heterodimer complex with DRAP1 through its histone fold domain. More recently it was discovered that Dr1-DRAP1 is a bi-functional basal transcription factor that differentially regulates gene transcription through DPE (downstream promoter elements) or TATA box motifs. It can stimulate transcription in vitro from Drosophila promoters containing DPEs, whereas it represses transcription from TATA-containing promoters.
SRP2124 Dr1 (NC2β, 19 kDa), GST tagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Dr1 is a general negative regulator of class II and class III gene expression. It binds to the basic repeat domain of TBP on promoter DNA and can prevent the RNA polymerase II holoenzyme, or its TFIIB and/or TFIIA subunits, from assembling into an initiation complex. Dr1 is phosphorylated in vivo and this modification affects its interaction with TBP. In addition, Dr1 interacts with the hyperphosphorylated form of Pol II and with the repression domain of the AREB6 repressor. Dr1 forms a heterodimer complex with DRAP1 through its histone fold domain. More recently it was discovered that Dr1-DRAP1 is a bi-functional basal transcription factor that differentially regulates gene transcription through DPE (downstream promoter elements) or TATA box motifs. It can stimulate transcription in vitro from Drosophila promoters containing DPEs, whereas it represses transcription from TATA-containing promoters.
SRP2027 E2F-1 (RBAP-1) human recombinant, expressed in insect cells, ≥70% (SDS-PAGE) E2F was originally identified as a transcription factor mediating the transcription of adenovirus E2 gene. It is a heterodimer composed of two structurally related subunits, termed E2F and DP. E2F is encoded by at least five genes, E2F-1 through E2F-5, and DP is encoded by at least two genes, DP-1 and DP-2. All these genes (E2F-1 through E2F-5, DP-1 and DP-2) have been considered as members of the E2F gene family because they have a number of common structural and functional characteristics. Among those members of the E2F family, E2F-1 was the first E2F gene cloned and characterized. The E2F-1 protein has been shown to interact with RB both in vitro and in vivo. Although the E2F proteins can function as transcription factors by themselves, they should be considered as RB-mediators as well because almost every functional response of RB protein(s) requires the presence of E2F protein(s).
E2410 E2F Transcription Factor 6 human histidine tagged, recombinant, expressed in E. coli E2F6 (E2F transcription factor 6) acts as a transcriptional repressor in a pocket-protein independent manner, and it is not transactivated and does not contain pocket-protein binding domains. Human parvovirus B19 (B19V) elevates E2F6 expression, thus, prevents cell division of human erythroid progenitors. HPV (human papilloma virus)16 E7 oncoprotein interacts with E2F6 and leads to the deregulation of its expression. It acts as an antagonist of E2F-1, which is pro-apoptotic in nature, and prevents the apoptosis of hematopoietic progenitor cells during proliferation. It interacts with BRCA1, through its C-terminal and suppresses the ultraviolet-induced apoptosis.
E2F6 is a member of the E2F family of transcription factors that play an important role in the regulation of cell cycle progression. In normal cells, E2F activity is regulated by binding to pRB, the product of the retinoblastoma gene, and by binding to "pocket proteins", p107 and p130.
SRP5161 4EBP1, GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5162 4EBP1, His tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5232 EIF2S1, His tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5179 ELK1, GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP2163 Estrogen Receptor human recombinant, expressed in insect cells, ≥80% (SDS-PAGE) Several members of the nuclear receptor family are directly associated with human malignancies including breast cancer, prostate cancer and leukemia. The pathogenesis of each of these diseases is underpinned by the activities of a member of the superfamily; estrogen receptor-alpha (ER alpha) in breast cancer, androgen receptor (AR) in prostate cancer, and retinoic acid receptor alpha (RAR alpha) in acute promyelocytic leukemia. Estrogen receptors (ER) are members of the superfamily of nuclear hormone receptors (2, 3) whose activity is required for the normal function of the female reproductive system. Two isoforms of estrogen receptor (ER α and ER β) have been described. They function as ligand-dependent transcriptional activators. The biological functions downstream of ER result from altered expression of direct transcriptional targets as well as secondary effects mediated by biological activities of direct targets. In the mammary gland, estrogen receptors regulate normal epithelial cell development and differentiation through their well-documented effects on transcription. Estrogens have long been known to have mitogenic functions in breast cancer cell lines and in breast tumors. Selective estrogen receptor modulatory compounds (SERMs), which bind directly to ER, can block the growth stimulatory function of estrogens.
E1528 Estrogen Receptor-α human ≥80% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution Hormone-inducible transcription factor capable of acting positively or negatively in regulating genes involved in tissue growth and differentiation. For use in signal transduction, steroid biochemistry, and endocrine disruptor research.
SRP2091 FGF-1 human recombinant, expressed in insect cells, ≥85% (SDS-PAGE) Acidic fibroblast growth factor (FGF-1) and basic fibroblast growth factor (FGF-2) are ubiquitous cytokines found in many tissues. They have effects on multiple cell types derived from mesoderm and neuroectoderm, including endothelial cells. FGF proteins are small peptides of 155 to 268 amino acid residues. The degree of sequence identity between different family members is 30-60 % in a "central domain" of approx. 120 amino acids. This domain confers to FGFs a common tertiary structure and the ability to bind to heparin. Secreted FGFs signal to target cells by binding and activating cell-surface tyrosine kinase FGF receptors (FGFRs; 6, 7). The function of FGFs and FGFRs during embryonic development and adult physiology has been addressed by gain- and loss-of-function experiments in several animal model organisms. These studies have shown that FGFs act as key regulators of developmental events.
The protein fibroblast growth factor 1, functions intracellularly to protect cells against stress. The protein functions as an angiogenic factor that participates in tissue repair, carcinogenesis, and maintenance of vasculature stability. Its expression is found to be upregulated in in patients with rheumatic arthritis. It serves as a prognostic biomarker in several cancers and a potential therapeutic target for patients with non-small cell lung cancer.
SRP5181 FOS, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP2087 C-fos, proto oncogene human recombinant, expressed in insect cells, ≥70% (SDS-PAGE) The transcription factor AP-1 (activator protein-1) is involved in cellular proliferation, transformation and death. AP-1 and nuclear factor B (NF B) can be specifically targeted to prevent cancer induction in mouse models. AP-1 can be produced by 18 different dimeric combinations of proteins from the Jun [c-Jun, JunB and JunD] and Fos (c-Fos, FosB, Fra-1 and Fra-2) families, including Jun homodimers and Jun-Fos heterodimers. The Jun and Fos proteins contain a basic-region leucine zipper (bZIP) domain, and are capable of binding to other bZIP proteins including those from the ATF, MAF, CNC and C/EBP (CCAAT/enhancer-binding protein) subfamilies. Jun-Jun and Jun-Fos dimers bind with highest affinity to the 12-O-tetradecanoylphorbol-13-acetate (TPA) response element (TRE) [TGA(C/G)TCA], although many other AP-1-like sites have been reported. Binding to any of these sites can be tissue-specific, or affected by neighboring sequences, and dependent upon interactions with other transcription factors or cofactors. Jun and Fos proteins can also dimerize with other bZIP proteins, allowing them to target other DNA binding sites, such as the cAMP response element (CRE), the antioxidant response elements (ARE), and half-sites composed of half of a TRE site and half of a MAF- or CNC-binding site. In addition, AP-1 proteins can interact with other proteins, including the p65 subunit of NF-B, CBP (CRE-binding-protein-binding protein) (p300), SMAD-3 and -4, and the retinoblastoma protein (see 5 for a more complete list), further increasing the combinatorial potential of Jun and Fos proteins. AP-1 regulates a variety of cellular processes, including proliferation, differentiation and apoptosis, and contributes to both basal and stimulus-activated gene expression. It is activated by growth factors, hormones, stress, cytokines, ROS and ultraviolet radiation. Activation occurs both transcriptionally and post-translationally, and is signaled predominantly through the mitogen-activated protein kinase (MAPK) cascade. The combinatorial diversity of AP-1 proteins and other interacting factors appears to influence how specific cell types respond to a stimulus.
SRP2094 Fos-related antigen 1 human recombinant, expressed in insect cells, ≥70% (SDS-PAGE) The fos-related antigen 1 (Fra-1, or FosL1: Fos-like antigen 1) is a member of the Fos onco-protein family and a component of AP-1 transcription factor. Similar to other members of the family, Fra-1 contains a leucine zipper domain and a highly conserved C-terminal region. Transcription of Fra-1 gene is regulated by multiple cis-elements and 12-O-tetradecanoylphorbol-13-acetate (TPA). Fra-1 expression is associated with proliferation and invasiveness of breast cancer cells and other cancer cells.
SRP2016 GAL4 [(1-147) - AH] from Saccharomyces cerevisiae recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Transcriptional activity is greatly stimulated by promoter-specific activator proteins. These are modular proteins, consisting of a DNA-binding domain and a regulatory (activator) domain. The GAL4 protein of yeast activates the transcription of several genes involved in galactose metabolism. This event requires that GAL4 bind to upstream activation sites with the consensus sequence 5′-CGGN5(T/A)N5CCG-3′ (5 ). A fragment of the GAL4 protein, comprising amino acids 1-147, binds DNA but fails to activate transcription. Linking of an acidic synthetic peptide, forming an α-helix (AH), to this GAL4 DNA-binding domain, results in a protein with an amphipathic structure. This fusion protein is able to activate transcription of a gene, bearing the GAL4 binding sites in an in vitro transcription system by targeting TFIIB in the pre-initiation complex.
SRP2018 GAL4 [(1-147) + E1A (121-223)] from Saccharomyces cerevisiae canine adenovirus recombinant, expressed in E. coli, ≥70% (SDS-PAGE) The GAL4 protein of yeast activates the transcription of several genes involved in galactose metabolism. This event requires that GAL4 bind to upstream activation sites with the consensus sequence 5`-CGGN5(T/A)N5CCG-3` . A fragment of the GAL4 protein, comprising amino acids 1-147, binds DNA but fails to activate transcription. The adenovirus E1A protein stimulates transcription of a wide variety of viral and cellular genes. In addition to its trans-activating functions, E1A is also able to modulate progression through the cell cycle, to immortalize primary cells in culture and to induce cellular transformation. The E1A protein binds to the TATA-binding protein, TBP, TAFII55 and TAFII110. Its activating domain has been shown to interact with E2F, ATF-2 and YY1.
SRP2017 GAL4 [(1-147) + VP16 (411-490)] from Saccharomyces cerevisiae human herpesvirus 2 recombinant, expressed in E. coli, ≥80% (SDS-PAGE) The GAL4 protein of yeast activates the transcription of several genes involved in galactose metabolism. This event requires that GAL4 bind to upstream activation sites with the consensus sequence 5′-CGGN5(T/A)N5CCG-3′ . A fragment of the GAL4 protein, comprising amino acids 1-147, binds DNA but fails to activate transcription. Herpes virus VP16 activates expression of immediate early genes in virally-infected cells. As most other eukaryotic transcriptional activator proteins, VP16 has a modular domain structure: it’s N-terminus is involved in DNA-protein interactions, while its C-terminal 79 amino acids have proven to be an especially potent transactivation domain. When fused to the DNA-binding domain of the yeast GAL4, this VP16 fragment functions as an activator of transcription in yeast, mammalian cells and in vitro transcription assays. VP16 has been shown to bind to TBP, TFIIB, and replication factor A.
The GAL4 yeast protein is responsible for the induction of various genes involved in galactose metabolism. This requires the binding of GAL4 gene to the upstream activation sites containing the consensus sequence 5′-CGGN5(T/A)N5CCG-3′. VP16 protein is essential for inducing the expression of viral immediate-early (IE) genes. A fragment of the GAL4 protein, comprising amino acids 1-147, binds DNA but fails to activate transcription. The highly acidic C-terminal tail of VP16 functions as a potent transcriptional activator in mammalian cells. GAL4-VP16 construct functions as an activator which promotes transcription in mammalian cells.
G1542 Glucocorticoid Receptor human recombinant, expressed in baculovirus infected insect cells, buffered aqueous solution Glucocorticoid Receptor (GR) acts upon and mediates the actions of glucocorticoids which are essential for normal physiological processes. In mothers with postnatal depression, this gene is methylated at the promoter in infants. This effect is suppressed by stroking of infants by their mothers. Various infectious disease-related genes in the GR signal transduction pathway are influenced by prenatal exposure to arsenic and cadmium.
SRP2099 HIF-1 α N-terminal activation domain (530-698) human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Hypoxia-inducible factor-1 (HIF1) is a transcription factor found in mammalian cells cultured under reduced oxygen tension that plays an essential role in cellular and systemic homeostatic responses to hypoxia. HIF1 is a heterodimer composed of an alpha subunit and a beta subunit. The beta subunit has been identified as the aryl hydrocarbon receptor nuclear translocator (ARNT). This gene encodes the alpha subunit of HIF-1. HIF-1α contains two transactivation domains located between amino acids 531 and 826. Overexpression of a natural antisense transcript (aHIF) of this gene has been shown to be associated with nonpapillary renal carcinomas. Two alternative transcripts encoding different isoforms have been identified. Specific disruption of the HIF-1 pathway is important for exploring its role in tumor biology and developing more efficient weapons to treat cancer. HIF-1alpha is a master regulator of the hypoxic response, and its proangiogenic activities include, but are not limited to, regulation of vascular endothelial growth factor (VEGF). HIF-1alpha protein expression often seen in invasive breast cancer. Recent data demonstrates that HIF-1alpha knockdown reduces tumorigenicity of MCF-7 cells and suggest a promising combination of both anti-HIF-1 strategy and traditional chemotherapy to improve cancer treatment.
SRP2097 HIF-1 α, C-terminal activation domain (776-826 human recombinant, expressed in E. coli, ≥85% (SDS-PAGE) During hypoxia, the two subunits of this factor undergo post-translational modifications which in turn promote transactivation.
Hypoxia-inducible factor-1 (HIF1) is a transcription factor found in mammalian cells cultured under reduced oxygen tension that plays an essential role in cellular and systemic homeostatic responses to hypoxia. HIF1 is a heterodimer composed of an alpha subunit and a beta subunit. The beta subunit has been identified as the aryl hydrocarbon receptor nuclear translocator (ARNT). This gene encodes the alpha subunit of HIF-1. HIF-1α contains two transactivation domains located between amino acids 531 and 826. Overexpression of a natural antisense transcript (aHIF) of this gene has been shown to be associated with nonpapillary renal carcinomas. Two alternative transcripts encoding different isoforms have been identified. Specific disruption of the HIF-1 pathway is important for exploring its role in tumor biology and developing more efficient weapons to treat cancer. HIF-1alpha is a master regulator of the hypoxic response, and its proangiogenic activities include, but are not limited to, regulation of vascular endothelial growth factor (VEGF). HIF-1alpha protein expression often seen in invasive breast cancer. Recent data demonstrates that HIF-1alpha knockdown reduces tumorigenicity of MCF-7 cells and suggest a promising combination of both anti-HIF-1 strategy and traditional chemotherapy to improve cancer treatment.
H4652 HMG-1 human lyophilized powder, ≥90% (SDS-PAGE), Histidine-tagged, recombinant, expressed in E. coli HMG-1 (high mobility group protein) is a non-histone chromosomal protein, which promotes the sequence specific DNA attachment of proteins. HMG1 binds DNA in a non-sequence specific manner. It is involved in DNA replication, transcription and repair. In addition, it is up-regulated in cancers and is associated with cellular growth, vasculogenesis and apoptosis regulation. In the presence of infection or injury, HMG1 is secreted and mediates inflammation. It is associated with the pathogenesis of autoimmune diseases, such as rheumatoid arthritis (RA), inflammatory bowel disease (IBD) and systemic lupus erythematosus (SLE).
SAB4200522 Anti-IDH1 (C-terminal) antibody produced in rabbit ~1.0 mg/mL, affinity isolated antibody  
C5859 c-Jun human 40-50% (SDS-PAGE), recombinant, expressed in E. coli, truncated human c-Jun sequence-GST fusion protein 1-169-GST, soluble Substrate for SAPK1/JNK2. Purified protein transcription factor which binds the AP1 gene to activate transcription.
SRP5176 c-JUN (1-79), GST tagged human recombinant, expressed in E. coli, ≥50% (SDS-PAGE), buffered aqueous glycerol solution  
SRP2088 C-jun, proto oncogene human recombinant, expressed in insect cells, ≥80% (SDS-PAGE) The transcription factor AP-1 (activator protein-1) is involved in cellular proliferation, transformation and death. AP-1 and nuclear factor B (NF- B) can be specifically targeted to prevent cancer induction in mouse models. AP-1 can be produced by 18 different dimeric combinations of proteins from the Jun (c-Jun, JunB and JunD) and Fos (c-Fos, FosB, Fra-1 and Fra-2) families, including Jun homodimers and Jun-Fos heterodimers. The Jun and Fos proteins contain a basic-region leucine zipper (bZIP) domain, and are capable of binding to other bZIP proteins including those from the ATF, MAF, CNC and C/EBP (CCAAT/enhancer-binding protein) subfamilies (5]) Jun-Jun and Jun-Fos dimers bind with highest affinity to the 12-O-tetradecanoylphorbol-13-acetate (TPA) response element (TRE) [TGA(C/G)TCA], although many other ′AP-1-like sites′ have been reported. Binding to any of these sites can be tissue-specific, or affected by neighboring sequences, and dependent upon interactions with other transcription factors or cofactors. Jun and Fos proteins can also dimerize with other bZIP proteins, allowing them to target other DNA binding sites, such as the cAMP response element (CRE), the antioxidant response elements (ARE), and half-sites composed of half of a TRE site and half of a MAF- or CNC-binding site. In addition, AP-1 proteins can interact with other proteins, including the p65 subunit of NF- B, CBP (CRE-binding-protein-binding protein) (p300), SMAD-3 and -4, and the retinoblastoma protein (see 5 for a more complete list), further increasing the combinatorial potential of Jun and Fos proteins. AP-1 regulates a variety of cellular processes, including proliferation, differentiation and apoptosis, and contributes to both basal and stimulus-activated gene expression. It is activated by growth factors, hormones, stress, cytokines, ROS and ultraviolet radiation Activation occurs both transcriptionally and post-translationally, and is signaled predominantly through the mitogen-activated protein kinase (MAPK) cascade. The combinatorial diversity of AP-1 proteins and other interacting factors appears to influence how specific cell types respond to a stimulus. The growth-promoting activity of c-Jun is mediated by repression of tumor suppressors, as well as up-regulation of positive cell cycle regulators. Mostly, c-Jun is a positive regulator of cell proliferation, whereas JunB has the converse effect.
SRP5219 KAT3A (518-1207), GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution KAT3A has intrinsic histone acetyltransferase activity that acts as a scaffold to stabilize additional protein interactions with the transcription complex and acetylates both histone and non-histone proteins. KAT3A (CREBBP) expressed as a nuclear protein that binds to cAMP-response element binding protein (CREB) and involved in the transcriptional coactivation of many different transcription factors. KAT3A plays a main role in embryonic development, growth control, and homeostasis by coupling chromatin remodeling to transcription factor recognition. KAT3A also plays a critical role in the transmission of inductive signals from cell surface receptors to the transcriptional apparatus.
SRP5198 KAT3B (532-1153), GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5211 KAT7, active, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5220 KAT8 (2-467), GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution Lysine acetyltransferase 8 (KAT8) or MYST histone acetyltransferase 1 (MYST1) was originally isolated as a human immunodeficiency virus-1 (HIV-1) TAT-interactive protein, which plays important roles in regulating chromatin remodeling, transcription and other nuclear processes by acetylating histone and non-histone proteins. MYST1 is also involved in ataxia-telangiectasia mutated (ATM) function. It acetylates histone 4-lysine 16 (H4K16). The protein is a modulator of embryonic stem cells and an epigenetic regulator. It has been associated with gastric carcinoma.
SRP5201 KAT9, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5221 KDM5C (1-671), GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP3101 KLF4-TAT human recombinant, expressed in HEK 293 cells, ≥90% (SDS-PAGE), ≥90% (HPLC), cell culture tested KLF4 is a member of the Kruppel-like factor (KLF) family of zinc finger transcription factors. Recombinant human KLF4-TAT is a 51.7 kDa protein containing 483 amino acid residues, including 13- residue C-terminal TAT peptide.
SRP3107 Lin28-TAT human recombinant, expressed in E. coli, ≥90% (SDS-PAGE), ≥90% (HPLC), cell culture tested Lin28 is a RNA-binding protein that belongs to a diverse family of structurally-related transcription factors. Recombinant human Lin28-TAT is a 24.4 kDa protein containing 222 amino acid residues, including 13- residue C-terminal TAT peptide.
SRP2070 LRH-1 human recombinant, expressed in insect cells, ≥70% (SDS-PAGE) LRH-1 or HB1F for human B1-binding factor belongs to the fushi tarazu factor-1 (FTZ-F1) subfamily of orphan nuclear receptors and is closely related to steroidogenic factor-1. LRH1 contains a DNA-binding domain with 2 zinc finger motifs, an FTZ-F1 box, and a ligand-binding domain. Cholesterol 7-α-hydroxylase is the first and rate-limiting enzyme in a pathway through which cholesterol is metabolized to bile acids. Elevated promoter-specific repressor protein (SHP) inactivates LRH1 by forming a heterodimeric complex that leads to promoter-specific repression of both CYP7A1 and SHP. These results revealed an elaborate autoregulatory cascade mediated by nuclear receptors for the maintenance of hepatic cholesterol catabolism. LRH1 specifically binds and activates viral hepatitis B enhancer II, an essential element for the liver-specific regulation of hepatitis B virus gene expression. CPF is a key regulator of human CYP7A gene expression in the liver. SHP1 represses expression of CYP7A1 by inhibiting the activity of LRH1 which regulates CYP7A1 expression positively. This bile acid-activated regulatory cascade provides a molecular basis for the coordinate suppression of CYP7A1 and other genes involved in bile acid biosynthesis.
SRP2145 LRH-1, GST tagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) LRH-1 (NR5A2) is expressed specifically in pancreas and liver, playing important roles in the regulation of several liver-specific genes. LRH-1 is a mammalian homologue of Drosophila fushi tarazu factor (dFTZ-F1) and structurally belongs to the orphan nuclear receptor superfamily. LRH-1 can recognize the DNA sequence 5′-AAGGTCA-3′, the canonical recognition motif for steroidogenic factor 1 (SF-1). Enhancer II (ENII) is one of the critical cis-elements in the Hepatitis B Virus (HBV) genome for the hepatic viral gene transcription and DNA replication. The liver-specific activity of ENII is regulated by multiple liver-enriched transcription factors, including LRH-1/hB1F. The role LRH-1 and dosage-sensitive sex reversal, adrenal hypoplasia congenital critical region on the X chromosome, gene 1 (DAX-1) in the regulation of StAR gene expression in human granulosa cell tumor cells has been investigated. LRH-1, is expressed in granulosa cells and has been shown to synergize with the cAMP signaling system to regulate the gonadal type II aromatase promoter in transient transfection assays. Observations support a direct role for LRH-1 in the induction of the progesterone but not the estrogen biosynthetic pathway during granulosa cell differentiation. The human nuclear receptor liver receptor homolog 1 (hLRH-1) plays an important role in the development of breast carcinomas. results indicate that hLRH-1′s control of gene expression is mediated by phospholipid binding, and establish hLRH-1 as a novel target for compounds designed to slow breast cancer development.
SRP2100 MAX dimerization protein 1 (MAD) human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) MAX dimerization protein belongs to a subfamily of MAX-interacting proteins. This protein competes with MYC for binding to MAX to form a sequence-specific DNA-binding complex, acting as a transcriptional repressor (while MYC appears to function as an activator) and is a candidate tumor suppressor. Both Myc and Mad, as well as the more recently described Mnt and Mga proteins, form heterodimers with Max, permitting binding to specific DNA sequences. These DNA-bound heterodimers recruit coactivator or corepressor complexes that generate alterations in chromatin structure, which in turn modulate transcription. The wild-type c-Myc and c-Myc/MadBR proteins have indistinguishable biological activity and target gene recognition in vivo.
SRP2095 MDM2, HIS tagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE), buffered aqueous solution Originally discovered as one of three genes amplified on double minute chromosomes in a tumorigenic derivative of NIH 3T3 cells, MDM2 was later shown to possess oncogenic potential when overexpressed. High-level expression of MDM2 has also been shown to confer tumorigenic potential upon nontransformed rodent fibroblasts in athymic nude mice. MDM2 can immortalize rat embryo fibroblasts and can cooperate with activated RAS to transform these cells. Elevated levels of MDM2 protein have been found in a variety of human tumors, most notably in soft tissue sarcomas where up to 30% of primary tumors contain multiple copies of the MDM2 gene. One mechanism by which MDM2 overexpression promotes tumor development is through its ability to bind to the p53 tumor suppressor, thereby blocking the transactivation, cell cycle arrest, and apoptotic functions of p53. MDM2 can inhibit p53 activity in a number of ways including preventing p53 from recruiting TAFs, promoting nuclear export, inhibiting p53 acetylation, and perhaps most importantly by virtue of its function as an E3 ubiquitin ligase with specificity for, among others, p53. In addition to regulating p53 levels by targeting p53 for proteasomal degradation MDM2 also transfers ubiquitin to itself, MDMX, the ß2 adrenergic receptor, glucocorticoid receptor, TIP60, and PCAF.
SRP2150 MKP3, GST tagged human recombinant, expressed in E. coli, ≥85% (SDS-PAGE) MKP3 (MAP (mitogen-activated protein) kinase phosphatase 3), or DUSP6 (dual specificity phosphatase 6), participates in one of the feedback loops regulating MAPK signal pathways in normal cell growth, where it dephosphorylates activated ERK (extracellular signal-regulated kinase) and inhibits growth-inducing signals. This protein localizes in the cytoplasm, and prevents ERK translocation to nucleus to act upon its effectors. In vitro studies in primary pancreatic cancer tissues show that this protein induces apoptosis and acts as a tumor suppressor gene. It acts as a negative feedback regulator of FGFR (fibroblast growth factor receptor) signaling, and mutations in this gene might be linked with unexplained FGFR-like syndrome cases. Expression levels of MKP3 gene in tumor samples might have potential as prognostic markers in non-small cell lung cancer (NSCLC), and the rs2279574 variant in MKP3 gene can help predict the chemoradiotherapy outcome in patients with inoperable NSCLC. In atypical endometrial hyperplasia (AEH), this gene can also help predict the effectiveness of progestin therapy.
The mitogen-activated protein kinase phosphatases (MKPs) are dual specificity phosphatases (DUSPs) that dephosphorylate phospho-Ser/Thr and phospho-Tyr residues. At least ten mammalian MPKs have been identified. MKPs have been studied for their important roles in MAPK related cancer cells and innate immune response. The MKP3, known as DUSP6 (dual specificity protein phosphatase 6), is a member of the protein tyrosine phosphatase superfamily. The MKP3 tightly regulates to ERK substrates by dephosphorylating both the phospho-Ser/Thr and phospho-Tyr residues. Its kinase interaction domain (KIM, residues 61-75) in addition to a conserved cytosolic domain (residues 161-177) and C-terminus domain (residues 348-381) plays an important role in ERK2 binding. Identification of specific activators or inhibitors of MKP3 and MPK1 may lead to the development of drug candidates against ERK pathway related diseases.
SRP2101 Myc-associated factor X (MAX) human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) The MAX gene encodes a protein that interacts specifically with the Myc protein to form a heterodimer with high affinity for the specific cognate DNA-binding site of Myc. The protein encoded by this gene is a member of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It is able to form homodimers and heterodimers with other family members, which include MAD, MXI1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms provides a complex system of transcriptional regulation. Substantial evidence has been accumulated over the last years that support the model that Myc/MAX/MAD proteins affect different aspects of cell behavior, including proliferation, differentiation, and apoptosis, by modulating distinct target genes. The unbalanced expression of these genes, e.g. in response to deregulated Myc expression, is most likely an important aspect of Myc`s ability to stimulate tumor formation. It is reported that in vivo transactivation assays suggest that Myc-MAX and MAD-MAX complexes have opposing functions in transcription and that MAX plays a central role in this network of transcription factors. High levels of MAX and stress-induced NFkappaB activation may result in elevated expression of Fas ligand in human lung cancer cells and possibly contribute to Fas ligand-associated immune escape mechanisms.
This protein has been associated with familial pheochromocytoma (PCC).
SRP2089 C-myc, proto oncogene human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) The universal deregulation of c-Myc gene expression in tumor cells suggests that this oncogene represents an attractive target for cancer therapeutic purposes. The c-Myc promoter integrates diverse mitogenic signaling cascades, which are constitutively activated in tumor cells, and translates them into expression of the c-Myc transcription factor, which promotes cell proliferation, growth, differentiation, and apoptosis by regulating the expression of numerous target genes. The structural and biochemical features of the MYC family (MYC, N-MYC, and L-MYC) mark them as direct regulators of gene expression. As basic helix-loop-helix leucine zipper proteins (bHLH-ZIP), the MYCs acquire the capacity to bind the DNA sequence CACGTG (E-box) when dimerized with MAX (another bHLH-ZIP, 4,5). A head-to-tail pair of MYC-MAX dimers may, in turn, form a heterotetramer capable of bridging distant E-boxes. Among the broadly distributed positive enforcers of MYC action that are often recruited to target genes are chromatin remodeling (SWI/SNF relatives) and modifying complexes (TRAPP/GCN5 and relatives); these complexes mobilize nucleosomes and acetylate histones and/or other targets to activate gene expression. MYC binds TBP along an auxiliary pathway to control gene expression. MAD and MNT generally oppose MYC action by enlisting histone deacetylase complexes. Besides acting at the level of chromatin, MYC may also operate at later stages of the transcription cycle, after pre-initiation complex formation. In addition to using generic chromatin complexes to up- or down-regulate transcription, the MYC network also conscripts individual factors to modify expression locally on an ad hoc basis. For example, YY1, AP2, MIZ1, SP1, BRCA1, and other proteins interact directly with MYC, and so may directly modify the output of the MYC network.
SAB4200539 Anti-Myocardin antibody produced in rabbit affinity isolated antibody  
SRP3119 NANOG human recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), cell culture tested NANOG is one of the central genes regulating self-renewal and pluripotency capacities of embryonic stem cells (ESC). Constitutive expression of this gene prevents the differentiation of ESCs, and along with SOX2 (SRY-box 4) and OCT-4 (octamer-binding transcription factor 4), it regulates pluripotency-related gene expression and maintains the pluripotency of ESCs. During ESC differentiation both these genes are down-regulated, and gene profiling shows that the expression of NANOG is uniformly high in ESC lines. There is significant similarity between ESC and carcinoma in situ testis (CIS), including the high expression of NANOG. It is novel marker for testicular CIS and germ cell tumors. NANOG shows abnormal expression in a variety of human cancers, such as carcinomas of the brain, oral cavity, head and neck, breast, lung, liver, pancreas, kidney, gastric, cervix, ovary, prostate, and colon. This expression is also related to treatment resistance and poor survival of cancer patients.
SRP3120 NANOG TAT human recombinant, expressed in E. coli, ≥95% (SDS-PAGE), ≥95% (HPLC), cell culture tested Nanog is a regulatory protein that is associated with undifferentiated pluripotent cells. Recombinant human Nanog-TAT is a 36.2 kDa protein, which is synthesized as a 304 amino acid polypeptide plus a 13- residue C-terminal TAT peptide.
SRP5104 NFATC1, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP0386 NSD1 human recombinant, expressed in E. coli, ≥63% (SDS-PAGE)  
SRP5110 P300 (1283-1673), GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP2025 p52 human recombinant, expressed in E. coli, ≥70% (SDS-PAGE) The human p52 protein is a non-TAF transcription coactivator that mediates activator-dependent transcription by RNA polymerase II. The function of p52 is through interactions with transcriptional activators and the basal transcription machinery. In addition, p52 may also interact with several cellular proteins including the transcription coactivator PC4, the essential splicing factor ASF/SF2 and the nuclear protein nucleolin.
SRP2078 p53 (1-342) C-terminal deletion human recombinant, expressed in insect cells, ≥80% (SDS-PAGE) Human p53 protein is composed of 393 amino acid residues with several distinct regions. The N-terminal activation domain allows p53 protein to recruit the basal transcription machinery and activate the expression of target genes. The core domain binds to target DNA in a sequence-specific manner and the majority of mutations found in human tumors occur in the region of the gene encoding this domain. The C-terminal domain is composed of predominantly basic residues and modification of the C-terminal basic domain, including acetylation, glycosylation and phosphorylation, is an essential mechanism for regulating p53 function. Disruption or loss of oligomerization function is associated with loss of cell cycle arrest. This mutant protein (with the deletion of the C-terminus 51 residues including the entire basic domain and a portion of the tetramerization domain) can be used as a unique tool to study specific functions of p53 related to the C-terminus.
SRP2108 p53 (1-81), mutant, GST tagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) The protein has the capability to induce cell cycle arrest and has a role in DNA repair, senescence and apoptosis. It binds to Simian vacuolating virus 40 (SV40) T-antigen and human papilloma virus E6 protein.
p53 was identified as a tumor suppressor by showing that this protein has the ability to block transformation and to inhibit tumor cell growth. In addition, p53 is a transcription factor capable of regulating the expression of a subset of downstream genes. Mutation of two specific N-terminal residues in p53 (residues Leu22 and Trp23) impairs the ability of p53 to transactivate and has been correlated with its ability to bind TAFII40 and TAFII60 (or TAFII31 and TAFII70) (7, 8) suggesting that one or both of these interactions is important for activation. Mutation of residues 22 and 23 to Ala does not affect binding to TBP, although mutation of these residues to charged amino acids has been reported to disrupt the p53-TBP interaction. Different mutations in p53 gene have been characterized in a variety of human cancers. Loss or mutation of p53 function is highly correlated with tumorigenesis.
SRP2107 p53 (1-81), wild type, GST tagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) p53 was identified as a tumor suppressor by showing that this protein has the ability to block transformation and to inhibit tumor cell growth. In addition, p53 is a transcription factor capable of regulating the expression of a subset of downstream genes. Mutation of two specific N-terminal residues in p53 (residues Leu22 and Trp23) impairs the ability of p53 to transactivate and has been correlated with its ability to bind TAFII40 and TAFII60 (or TAFII31 and TAFII70) suggesting that one or both of these interactions is important for activation. Mutation of residues 22 and 23 to Ala does not affect binding to TBP, although mutation of these residues to charged amino acids has been reported to disrupt the p53-TBP interaction. Different mutations in p53 gene have been characterized in a variety of human cancers. Loss or mutation of p53 function is highly correlated with tumorigenesis.
SRP5113 p73a, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5114 P73b, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5115 P73g, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP2026 p75 human recombinant, expressed in E. coli, ≥70% (SDS-PAGE) The human p75 protein, similar to p52, is a non-TAF transcription coactivator that mediates activator-dependent transcription by RNA polymerase II in vitro through most tested activators. Although p75 and p52 are derived from alternatively splicing of a single gene and share most coding sequence, they reveal different function in several aspects. In addition to functioning as a transcription coactivator, p75 has been shown to be involved in growth of epithelial cells as a lens epithelial cell-derived growth factor (LEDGF), and in pathogenesis of atopic dermatitis as an autoantigen.
SRP2052 p75-CTR (C-terminal region) human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Lens epithelium-derived growth factor (LEDGF, also known as p75) has been shown to enhance survival of lens epithelial cells (LECs) against stress. LEDGF is a transcriptional activator. It protects the cells by binding to cis-stress response ((A/T)GGGG(T/A)), and heat shock (HSE; nGAAn) elements in the stress genes and activating their transcription. Originally, it was isolated as a co-activator required for transcriptional activation in human cell-free systems containing RNA polymerase II and general initiation factors. LEDGF is expressed at all stages of development in a variety of organs and tissues. A second protein product, p52, can be produced from the same gene due to alternative splicing of pre-mRNA. in vitro, p52 was found to be more general and stronger transcriptional co-activator than LEDGF/p75. HIV-1 integrase (IN) forms a specific nuclear complex with p75 but not with p52, suggesting a role for p75’s C-terminal region in retroviral integration.
p75 and p52 proteins associate with chromatin tightly and interact with other nuclear proteins, out of which multiple proteins are anchored by p75 to the chromatin fiber. Therefore, these proteins are involved in transcriptional regulation. Lentiviruses utilize the chromatin tethering capacity of this protein to integrate into the host chromosomes. p75 not only anchors HIV (human immunodeficiency virus) integrase to chromatin and prevents its degradation, but also promotes the genome-wide HIV integration. Human papillomavirus (HPV) E6/E7 oncogenes promote the expression of p75 in host cells, which in turn confers protection to HPV-positive cancer cells against different types of cellular stress, such as DNA damage.
SRP2023 PC4, F77P mutant human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Human PC4 is a non-TAF transcription coactivator that mediates activator-dependent transcription by RNA polymerase II in vitro through most tested activators. The function of PC4 is through interactions with transcriptional activators and the basal transcription machinery. It is negatively regulated by casein kinase II phosphorylation both in vitro and in vivo. PC4 strongly binds single stranded DNA and the region essential for the single stranded DNA binding activity was mapped around residue 77. A single amino acid change at position 77 (F to P) abolishes both ds- and ss-DNA binding activity.
SRP2024 PC4, serine mutations human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Human PC4 is a non-TAF transcription coactivator that mediates activator-dependent transcription by RNA polymerase II in vitro through most tested activators. The function of PC4 is through interactions with transcriptional activators and the basal transcription machinery. It is negatively regulated by casein kinase II phosphorylation both in vitro and in vivo. PC4 strongly binds single stranded DNA and the region essential for the single stranded DNA binding activity was mapped around residue 77. A single amino acid change at position 77 (F to P) abolishes both ds- and ss-DNA binding activity.
SRP2022 PC4, wild type human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) It plays an important role in DNA damage repair, replication and cellular transformation. It also has a role in the organization of the chromatin. The protein has been shown to be overexpressed in astrocytoma.
The human PC4 is a non-TAF transcription coactivator that mediates activator-dependent transcription by RNA polymerase II in vitro through most tested activators. The function of PC4 is apparently through interactions with transcriptional activators and the basal transcription machinery. It is negatively regulated by casein kinase II phosphorylation both in vitro and in vivo. PC4 strongly binds single stranded DNA and regulates HSSB (RPA)-dependent SV40 DNA replication. Recent studies indicated that PC4 can be acetylated by several histone acetyltransferases.
SRP5116 PCAF (431-end), GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5117 PCNA, His tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP2054 PPARα, ligand binding domain (170-468) human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) There is evidence that a group of closely related nuclear receptors, called peroxisome proliferator-activated receptors (PPARs), may be involved in chronic diseases such as diabetes, obesity, artherosclerosis and cancer. The PPARs were first cloned as the nuclear receptors that mediate the effects of synthetic compounds called peroxisome proliferators on gene transcription. It soon became clear that eicosanoids and fatty acids can also regulate gene transcription through PPARs. They bind a specific element in the promoter region of target genes only as a heterodimer with the receptor for 9- cis retinoic acid, RXR (retinoid X receptor). Binding of the ligand of either receptor can activate the complex, but binding of both ligands simultaneously is more potent. Three PPAR isotypes have been identified: α, β (δ) (also called NUC1) and γ. PPARα is expressed most in brown adipose tissue and liver, then kidney, heart and skeletal muscle. PPARγ is mainly expressed in adipose tissue, and to a lesser extent in colon, the immune system and the retina. PPARβ is found in many tissues but the highest expression is in the gut, kidney and heart. The target genes of PPARα are a relatively homogenous group of genes that participate in aspects of lipid catabolism such as fatty acid uptake through membranes, fatty acid binding in cells, fatty acid oxidation (in microsomes, peroxisomes and mitochondria) and lipoprotein assembly and transport.
SRP2158 Pregnane X Receptor human recombinant, expressed in insect cells, ≥80% (SDS-PAGE) The nuclear pregnane X receptor (PXR; NR1I2) is an important component of the body′s adaptive defense mechanism against toxic substances including foreign chemicals (xenobiotics). PXR is activated by a large number of endogenous and exogenous chemicals including steroids, antibiotics, antimycotics, bile acids, and the herbal antidepressant St. John′s wort. PXR is known to regulate the expression of several additional genes encoding proteins involved in xenobiotic metabolism, including multidrug resistance protein 1 (MDR1), multidrug resistance-associated protein 2 (MRP2), and organic anion transporter polypeptide 2. Elucidation of the three-dimensional structure of the PXR ligand binding domain revealed that it has a large, spherical ligand binding cavity that allows it to interact with a wide range of hydrophobic chemicals. Thus, unlike other nuclear receptors that interact selectively with their physiological ligands, PXR serves as a generalized sensor of hydrophobic toxins. PXR binds as a heterodimer with the 9-cis retinoic acid receptor (NR2B) to DNA response elements in the regulatory regions of cytochrome P450 3A monooxygenase genes and a number of other genes involved in the metabolism and elimination of xenobiotics from the body. Although PXR evolved to protect the body, its activation by a variety of prescription drugs represents the molecular basis for an important class of harmful drug-drug interactions. Thus, assays that detect PXR activity will be useful in developing safer prescription drugs.
SRP2076 Pregnane X receptor (138-434), His tagged human recombinant, expressed in E. coli, ≥85% (SDS-PAGE) The nuclear pregnane X receptor (PXR; NR1I2) is an important component of the body’s adaptive defense mechanism against toxic substances including foreign chemicals (xenobiotics). PXR is activated by a large number of endogenous and exogenous chemicals including steroids, antibiotics, antimycotics, bile acids, and the herbal antidepressant St. John’s wort. PXR is known to regulate the expression of several additional genes encoding proteins involved in xenobiotic metabolism, including multidrug resistance protein 1 (MDR1) (8,9), multidrug resistance-associated protein 2 (MRP2) (10,11), and organic anion transporter polypeptide 2. Elucidation of the three-dimensional structure of the PXR ligand binding domain revealed that it has a large, spherical ligand binding cavity that allows it to interact with a wide range of hydrophobic chemicals. Thus, unlike other nuclear receptors that interact selectively with their physiological ligands, PXR serves as a generalized sensor of hydrophobic toxins. PXR binds as a heterodimer with the 9-cis retinoic acid receptor (NR2B) to DNA response elements in the regulatory regions of cytochrome P450 3A monooxygenase genes and a number of other genes involved in the metabolism and elimination of xenobiotics from the body.
SRP2090 RAD51 human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Properly controlled recombination between homologous DNA molecules (Homologous Recombination - HR) is essential for the maintenance of genome stability and for the prevention of tumorigenesis. RAD51 is a mammalian homologue of yeast RAD51 and bacterial RecA and, like its counterparts, plays a central role in HR. RAD51 coats ssDNA to form a nucleoprotein filament that invades and pairs with a homologous region in duplex DNA. It can then activate strand exchange to generate a crossover between the juxtaposed DNA molecules. In addition to RAD51, these steps require the coordinated action of a number of other homologous-recombination proteins, including the RP-A protein, which binds single-stranded DNA, RAD52, which can bind DNA ends, anneal complementary single-stranded DNA molecules and enhance the specificity of RAD51, and a number of RAD51 paralogs. The tumour-suppressor proteins BRCA1 and BRCA2 colocalize with RAD51 in DNA-damage-induced nuclear foci. BRCA2 has been shown to interact directly with RAD51 and thus plays a direct role in repair by HR, through control of the availability and function of the central mediator, RAD51.
RAD51 interacts with BRCA2 (breast cancer susceptibility protein) and participates in DSB (double strand DNA breaks) repair. BRCA2 sequesters and recruits RAD51 to the site of the damage and promotes the formation of the helical RAD51–single stranded DNA (ssDNA) nucleoprotein filaments. These filaments look for and infiltrate the homologous DNA template, and promote homologous recombination by inducing DNA polymerization and strand exchange. A dominant-negative mutation in this gene is linked with a novel Fanconi anaemia (FA) subtype, a disorder characterized by developmental abnormalities, bone marrow failure and a strong susceptibility to cancer. Association of RAD51 gene with congenital mirror movement disorders signifies the importance of RAD51-mediated homologous recombination in neurodevelopment apart from in DNA repair, cancer susceptibility.
SRP5125 Rel B, His tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP2081 Retinoblastoma protein human recombinant, expressed in insect cells, ≥70% (SDS-PAGE) pRB, the product of retinoblastoma susceptibility gene RB-1, is one of the best-studied tumor suppressor gene products. At least two other pRB-related proteins, p107 and p130, have been identified and characterized. Mutations in RB-1 gene are often associated with the occurrence of various tumors. The activity of pRB is regulated through phosphorylation in a cell cycle-dependent manner. The hyperphosphorylated RB protein usually associates with the cell nucleus and binds transcription factors of the E2F family. pRB represses transcription of its target genes, such as cdc2, cyclin A, and oncogene c-Myc, c-Fos through the binding with E2F factors and thereby regulating cell proliferation.
SRP2015 RNA Polymerase II, p14.5 subunit human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) hRPB9 is a subunit unique to RNA polymerase II, although it has sequence homologues in RNA polymerases I and III. The gene for Rpb9 is not essential for yeast cell viability, but is essential in Drosophila. hRPB9 has roles in both transcription initiation and transcription elongation. In the initiation reaction it is necessary for accurate start site selection. In the elongation reaction, RPB9, along with TFIIS facilitates the conversion of an arrest-competent conformation to a read-through competent conformation. RNA polymerase II lacking the RPB9 subunit uses alternate transcription initiation sites in vitro and in vivo and is unable to respond to the transcription elongation factor TFIIS in vitro. A role in the modulation of initiation and elongation is consistent with the localization of RPB9 in the three-dimensional structure of yeast RNA polymerase II. RPB9 is located at the tip of the so-called "jaws" of the enzyme, which is thought to function by clamping the DNA downstream of the active site. RPB9 comprises two zinc ribbon domains joined by a conserved linker region. The C-terminal zinc ribbon is similar in sequence to that found in TFIIS.
SRP2117 RNA Polymerase II, p14.5 subunit, GST tagged human recombinant, expressed in E. coli, ≥85% (SDS-PAGE) hRPB9 is a subunit unique to RNA polymerase II, although it has sequence homologues in RNA polymerases I and III. The gene for Rpb9 is not essential for yeast cell viability, but is essential in Drosophila. hRPB9 has roles in both transcription initiation and transcription elongation. In the initiation reaction it is necessary for accurate start site selection. In the elongation reaction, RPB9, along with TFIIS facilitates the conversion of an arrest-competent conformation to a read-through competent conformation. RNA polymerase II lacking the RPB9 subunit uses alternate transcription initiation sites in vitro and in vivo and is unable to respond to the transcription elongation factor TFIIS in vitro. A role in the modulation of initiation and elongation is consistent with the localization of RPB9 in the three-dimensional structure of yeast RNA polymerase II. RPB9 is located at the tip of the so-called "jaws" of the enzyme, which is thought to function by clamping the DNA downstream of the active site. RPB9 comprises two zinc ribbon domains joined by a conserved linker region. The C-terminal zinc ribbon is similar in sequence to that found in TFIIS.
SRP2116 RNA Polymerase II, p15.6 subunit, GST tagged human recombinant, expressed in E. coli, ≥85% (SDS-PAGE) hRPB6 is a highly conserved subunit shared by all three RNA polymerases, consisting of 142 amino acid residues. The gene for yeast RPB6 is essential for cell viability and homologues of this subunit exist in archaeal and some viral RNA polymerases. For example the bacterial w (the fifth subunit of the bacterial RNAP core enzyme) and eukaryotic RPB6 are structural homologs. RPB6 has been shown to promote pol II complex assembly, and/or increase its stability, through specific interactions with the largest subunit of RNA pol II. In addition, RPB6 was found to make contact with three small subunits, RPB5, RPB7, and RPB8 and to play a role in the interaction between RNA polymerase II and the transcription elongation factor TFIIS.
SRP2014 RNA Polymerase II, p33 subunit human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) hRPB3 (p33) is a highly conserved subunit shared by all three RNA polymerases. It has been shown to be in close contact to promoter DNA when pol II is recruited into the preinitiation complex. RPB3 has also been implicated in direct protein-protein contacts with transcription factor IIB, Rap30 subunit of transcription factor IIF, and gene-specific modulator proteins, such as the hepatitis B virus transactivator protein X or an inhibitor of pol II, RMP (RPB3-mediating protein). Therefore, RPB3 is facilitating the communication between the pol II core and a variety of basal and gene-specific transcription factors. In the pol II complex, RPB3 interacts with RPB5 and the RPB3–RPB5 interaction is intensified in the presence of three subunits, RPB7, RPB8 and RPB11. RPB3 also makes direct contacts with both RPB1 and RPB2, the two large subunits of the polymerase complex.
SRP2115 RNA Polymerase II, p33 subunit, GST tagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) In human, RPB3 is encoded by the POLR2C gene. This gene encodes the third largest subunit of RNA polymerase II. The product of this gene contains a cysteine rich region and exists as a heterodimer with another polymerase subunit, POLR2J. These two subunits form a core subassembly unit of the polymerase. DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Pol II is the central component of the basal RNA polymerase II transcription machinery. RPB3 is part of the core element with the central large cleft and the clamp element that moves to open and close the cleft. In the pol II complex, RPB3 interacts with RPB5 and the RPB3-RPB5 interaction is intensified in the presence of three subunits, RPB7, RPB8 and RPB11. Besides, RPB3 also interacts with RPB. RPB3 is involved in tissue-specific transcription and muscle differentiation via interaction with the myogenic factor Myogenin. RPB3 also interact with IGFBP3.
SRP2118 RNA Polymerase II, RPB10 subunit, GST tagged human recombinant, expressed in E. coli, ≥85% (SDS-PAGE) The RNA polymerase subunit RPB10 displays a high level of conservation across archaea and eukarya and is required for cell viability in yeast. It is a zinc-binding protein with an atypical CX2CXnCC metal binding motif. RPB10 participates in protein-protein interactions with additional components of the polymerase holoenzyme. Experimentally, the binding of RPB10 to an RPB3-RPB11 (or RPAC40-RPAC19 in RNAPI/III) heterodimer is well characterized and persists in both eukaryal and archaeal RNAPs. Binding of RPB10 to this a2-like heterodimer through zinc-mediated hemi-coordination suggests an early role in holoenzyme assembly since the formation of the α2-complex is the first step in the assembly of the prokaryotic RNAPs.
SRP2119 RNA Polymerase II, RPB12 subunit, GST tagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) RPB12 (also called RPB10 ) is shared between all three RNA polymerases and is homologous to the archaeal P subunit of RNA polymerase. Like RPB10, it is essential for yeast cell viability. RPB12 is also a zinc-binding protein with a canonical tetra-coordinating zinc motif but binds zinc in vitro much less efficiently than the RPB10 subunit. It has been shown to interact with both RPB1 and RPB2 in vitro and the human subunit can functionally substitute for its yeast counterpart.
SRP2110 RNA Polymerase II, RPB8 subunit, GST tagged human recombinant, expressed in E. coli, ≥85% (SDS-PAGE)  
SRP2013 RNA Polymerase II, C-terminal human recombinant, expressed in E. coli, ≥85% (SDS-PAGE) The carboxy-terminal repeat domain (CTD) of the largest subunit of RNA pol II contains tandem repeats of a heptapeptide sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser which is highly conserved among eukaryotic organisms. There are two forms of RNA pol II in vivo, designated IIO, which is extensively phosphorylated at the CTD, and IIA, which is not phosphorylated. The IIA form preferentially enters the pre-initiation complex (PIC), whereas IIO is found in the elongating complex. The kinase activity of TFIIH can mediate CTD phosphorylation, although other kinases, including Cdc2, Ctk1, the Srb10-Srb11 kinase-cyclin pair, and P-TEFb, have also been implicated in CTD phosphorylation. A phosphatase responsible for the dephosphorylation of the CTD has also been identified. CTD phosphatase activity is regulated by TFIIB and TFIIF. The CTD has also been implicated in pre-mRNA processing, most likely functioning as a platform for the recruitment and assembly of factors involved in pre-mRNA processing.
SRP2120 RNA Polymerase II, C-terminal domain, GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE) The CTD works as a binding scaffold for nuclear factors through its phosphorylation. It is suggested to be also involved in chromatin structure modification, DNA damage/repair, protein degradation and synthesis, RNA degradation, snRNA (small nuclear RNA) modification, and snoRNP (small nucleolar ribonucleoprotein) biogenesis.
The carboxy-terminal repeat domain (CTD) of the largest subunit of RNA pol II contains tandem repeats of a heptapeptide sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser which is highly conserved among eukaryotic organisms. There are two forms of RNA pol II in vivo: IIO, which is extensively phosphorylated at the CTD, and IIA, which is not phosphorylated. The IIA form preferentially enters the pre-initiation complex (PIC), whereas IIO is found in the elongation complex. The kinase activity of TFIIH can mediate CTD phosphorylation, although other kinases, including Cdc2, Ctk1, the Srb10-Srb11 kinase-cyclin pair, and P-TEFb, have also been implicated in CTD phosphorylation. A phosphatase responsible for the dephosphorylation of the CTD has also been identified. CTD phosphatase activity is regulated by TFIIB and TFIIF. The CTD has also been implicated in pre-mRNA processing, most likely functioning as a platform for the recruitment and assembly of factors involved in pre-mRNA processing.
SRP2125 RXRα, ligand binding domain, (200-462), GST tagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Retinoid X receptor (RXR) serves as a promiscuous heterodimerization partner for many nuclear receptors through the identity box, a 40-amino acid subregion within the ligand binding domain (LBD). RXR partners include thyroid hormone receptors (TRs), retinoic acid receptors (RARs), peroxisome proliferator-activated receptor, several constitutive active orphan nuclear receptors (e.g. nuclear growth factor I-B), oxysterol receptors, and constitutive androstane receptors. RXRs also form homodimers to mediate the effects of 9-cis-retinoic acid (9-cRA). Depending on these protein-protein interactions, RXR-containing complexes have distinct ligand-dependent and constitutive functions. The LBD is functionally complex and mediates ligand binding, receptor homo- and heterodimerization, repression of transcription in the absence of ligand, and ligand-dependent activation of transcription. Hormone binding to the structurally conserved LBD of the RXR triggers a conformational change that principally affects the conserved C-terminal transactivation helix H12 involved in transcriptional activation. Coactivators directly recruited by liganded receptors include members of the steroid receptor coactivator/p160 family such as SRC-1, transcriptional intermediary factor 2/glucocorticoid receptor interacting protein 1, and RAC3/activator of thyroid and retinoic acid receptors/amplified in breast cancer 1.
SRP2105 SC35 human recombinant, expressed in insect cells, ≥80% (SDS-PAGE) SC35, a member of the SR protein family, is an essential pre-mRNA splicing factor and can function as an essential splicing factor as well as an alternative splicing factor. Phosphorylation of serine residues located within the SR domain directly regulates SC35 activity and compartmentalization of other SR splicing factors. In addition to interacting with RNA and other splicing factors, SC35 has been shown to interact either directly or indirectly with the C-terminal domain (CTD) of the largest subunit of RNA polymerase II, thereby suggesting a potential role of SC35 in coordinating transcription and pre-mRNA splicing.
SRP5132 SMAD3, GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5133 SMAD4, GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5134 SMAD5, GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5215 SMYD3, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SAB4200472 Monoclonal Anti-SOX11 antibody produced in mouse ~1.0 mg/mL, clone SOX11-2, purified immunoglobulin  
SAB4200450 Anti-SOX11 (C-terminal) antibody produced in rabbit IgG fraction of antiserum  
SRP3157 Sox2 human recombinant, expressed in E. coli, ≥95% (SDS-PAGE), ≥95% (HPLC), cell culture tested Sox2 (sex determining region Y (SRY)-box 2) transcription factor participates in maintaining self-renewal and pluripotency of embryonic stem cells. The expression of this protein is aberrant in various human malignancies, and it acts as an oncogene in esophageal squamous cell carcinoma (SCC). SOX2 promotes proilferation, migration and adhesion abilities of dental pulp stem cells (DPSCs), and this might have applications in tissue engineering. It participates in Ewing′s sarcoma cell proliferation, and its inactivation results in apoptosis and G1/S arrest, in a PI3K (phosphoinositide 3-kinase)/Akt pathway-mediated manner.
SRP3158 Sox2 TAT human recombinant, expressed in E. coli, ≥95% (SDS-PAGE), ≥95% (HPLC), cell culture tested Sex determining region Y (SRY)-box 2 (SRY-2) or Sox2 plays an essential role in maintaining the pluripotency of embryonic stem cells (ESC) and determination of cell fate. Sox2 acts as a transcriptional activator after forming a ternary complex with Oct3/4 and a conserved non-coding DNA sequence (CNS1) located approximately 2kb upstream of the RAX promoter. The protein modulates stem cell function in embryonic and neural stem cells. Microarray analysis showed that Sox2 regulates the expression of multiple genes involved in embryonic development including fibroblast growth factor-4 (FGF-4), YES1 (a tyrosine-protein kinase) and ZFP206 (a transcription factor). Sox2 and other transcription factors have been introduced into cells by DNA transfection, viral infection, or microinjection. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing transcription factors and other nuclear proteins into primary as well as transformed cells.
SRP2029 Sp1 GC-box binding protein human ≥70% (SDS-PAGE) Sp1 was first detected in HeLa cells on the basis of its ability to activate the SV40 early promoter transcription. Subsequently it was shown to recognize and bind selectively to a GC-rich consensus sequence (GC-box: GGGCGG or CACCC) that presents in the promoter of several important cellular genes, including SV40 early, HIV-1, PDGF-B etc. Sp1 was the first transcription factor to be cloned. Analysis of structure and function has revealed that Sp1 can be separated into discrete functional domains. The DNA-binding domain consists of three zinc fingers that specifically bind to the GC-box element. Sp1 contains at least four separate transcriptional activation domains. Two of these domains are glutamine-rich, a well-characterized motif found in several other transcription factors. In addition to transcription, Sp1 function has been linked to cell growth, cancer, Huntington disease and other disorders through transcriptional regulation or specific protein-protein interactions. The function of Sp1 can be regulated by phosphorylation and glycosylation.
SRP2030 Sp1 GC-box binding protein human recombinant, expressed in insect cells, ≥75% (SDS-PAGE) Sp1 was first detected in HeLa cells on the basis of its ability to activate the SV40 early promoter transcription. Subsequently it was shown to recognize and bind selectively to a GC-rich consensus sequence (GC-box: GGGCGG or CACCC) that presents in the promoter of several important cellular genes, including SV40 early, HIV-1, PDGF-B etc. Sp1 was the first transcription factor to be cloned and characterized. Analysis of structure and function has revealed that Sp1 can be separated into discrete functional domains. The DNA-binding domain consists of three zinc fingers that specifically bind to the GC-box element. Sp1 contains at least four separate transcriptional activation domains. Two of these domains are glutamine-rich, a well-characterized motif found in several other transcription factors. In addition to transcription, Sp1 function has been linked to cell growth, cancer, Huntington disease and other disorders through transcriptional regulation or specific protein-protein interactions. The function of Sp1 can be regulated by phosphorylation and glycosylation.
SRP2123 Sp1 (GC-box binding protein), GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE) Sp1 binds to GC-rich sequences in a wide variety of promoters. It interacts with cell type or stage-specific transcription factors, and thus, regulates transcription of specific genes. It also controls the formation of the transcription initiation complex. This protein plays a key role in controlling the basal levels of glutathione S-transferase (GSTP1) promoter and the expression of leukotriene C4 synthase gene in the THP-1, a monocyte-like cell line.
Sp1 was first detected in HeLa cells on the basis of its ability to activate the SV40 early promoter transcription. Subsequently it was shown to recognize and bind selectively to a GC-rich consensus sequence (GC-box: GGGCGG or CACCC) that presents in the promoter of several important cellular genes, including SV40 early, HIV-1, PDGF-B etc. Sp1 was the first transcription factor to be cloned and. Analysis of structure and function has revealed that Sp1 can be separated into discrete functional domains. The DNA-binding domain consists of three zinc fingers that specifically bind to the GC-box element. Sp1 contains at least four separate transcriptional activation domains. Two of these domains are glutamine-rich, a well-characterized motif found in several other transcription factors. In addition to transcription, Sp1 function has been linked to cell growth, cancer, Huntington disease and other disorders through transcriptional regulation or specific protein-protein interactions. The function of Sp1 can be regulated by phosphorylation and glycosylation.
SRP2064 SRC1 (627-786), biotin,His tagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Steroid receptor coactivator 1 (SRC1) is a transcriptional coactivoator that mediates the activating functions of many of the nuclear hormone receptors. It is also known as NCoA1 and is a member of the SRC/p160 coactivator family. SRC1 has been shown to be over expressed in some cancers. SRC1 is a 160 kDa protein that contains several LXXLL motifs, which are involved in nuclear receptor interaction. The region 627-786 contains 3 LXXLL motifs that are involved in interaction with nuclear hormone receptorsand has been previously used in assays detecting ligand-dependent receptor-cofactor interactions. This protein does not contain any tag and will be useful for assays where a native untagged protein is desired.
SRP2066 SRC1 (627-786), biotin, untagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Steroid receptor coactivator 1 (SRC1) is a transcriptional coactivator that mediates the activating functions of many of the nuclear hormone receptors. It is also known as NCoA1 and is a member of the SRC/p160 coactivator family. SRC1 has been shown to be over expressed in some cancers. SRC1 is a 160 kDa protein that contains several LXXLL motifs, which are involved in nuclear receptor interaction. The region 627-786 contains 3 LXXLL motifs that are involved in interaction with nuclear hormone receptorsand has been previously used in assays detecting ligand-dependent receptor-cofactor interactions. This protein does not contain a His tag and will be useful for assays where a native untagged protein is desired. Lane 1 corresponds to 6His-tagged and biotinylated SRC-RID; Lane 2 corresponds to biotinylated SRC-RID without 6His tag.
SRP2065 SRC1 (627-786),His tagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Steroid receptor coactivator 1 (SRC1) is a transcriptional coactivator that mediates the activating functions of many of the nuclear hormone receptors. It is also known as NCoA1 and is a member of the SRC/p160 coactivator family. SRC1 is a 160 kDa protein that contains several LXXLL motifs, which are involved in nuclear receptor interaction. The region 627-786 contains 3 LXXLL motifs that are involved in interaction with nuclear hormone receptors and has been previously used in assays detecting ligand-dependent receptor-cofactor interactions.
SRP2069 SRC1, untagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Steroid receptor coactivator 1 (SRC1) is a transcriptional coactivator that mediates the activating functions of many of the nuclear hormone receptors. It is also known as NCoA1 and is a member of the SRC/p160 coactivator family. SRC1 has been shown to be over expressed in some cancers. SRC1 is a 160 kDa protein that contains several LXXLL motifs, which are involved in nuclear receptor interaction. The region 627-786 contains 3 LXXLL motifs that are involved in interaction with nuclear hormone receptorsand have been previously used in assays detecting ligand-dependent receptor-cofactor interactions. This protein is not tagged and will be useful for assays where a native untagged protein is desired.
SRP5137 STAT1 β, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP2063 STAT2 human recombinant, expressed in insect cells, ≥80% (SDS-PAGE) The signal transducer and activator of transcription (STAT) proteins play a crucial role in the regulation of gene expression by mediating transcriptional responses to many cytokines and growth factors. The antiviral responses of IFN-α/β rely on the transcriptional activities of STAT1 and STAT2 proteins. The chromatin immunoprecipitation and DNA microarray analysis (Chip-chip) demonstrated that STAT2 (and STAT1) bound to chromosome 22 after IFN stimulation. STAT2 activity can be regulated by tyrosine phosphorylation that is catalyzed by a receptor associated JAK kinase.
SRP2157 STAT4 human recombinant, expressed in insect cells, ≥85% (SDS-PAGE) Signal transducer and activator of transcription (STAT) proteins are a family of latent cytoplasmic transcription factors involved in cytokine, hormone, and growth factor signal transduction. Seven members of the STAT family of transcription factors have been identified in mammalian cells: STAT1, STAT2, STAT3, STAT4, STAT5a, STAT5b, and STAT6. STAT proteins mediate broadly diverse biologic processes, including cell growth, differentiation, apoptosis, fetal development, transformation, inflammation, and immune response. Receptor-recruited STATs are phosphorylated on a single tyrosine residue in the carboxy terminal portion. The modified STATs are released from the cytoplasmic region of the receptor subunits to form homodimers or heterodimers through reciprocal interaction between the phosphotyrosine of one STAT and the SH2 domain of another. Following dimerization, STATs rapidly translocate to the nucleus and interact with specific regulatory elements to induce target gene transcription. Recently, STAT-1 has been implicated in modulating pro- and anti-apoptotic genes following several stress-induced responses. These effects are dependent on STAT-1 phosphorylation on serine-727 and require the C-terminal transactivation domain of STAT-1 to enhance its pro-apoptotic effect or inhibit its anti-apoptotic effects. The STAT-1 C-terminal domain has been demonstrated to be important for protein-protein interaction with other transcriptional activators. The reports that STAT-1-deficient mice develop spontaneous and chemically induced tumours more rapidly compared to wild-type mice and that STAT-1-deficient cells are more resistant to agents that induce apoptosis strongly support the argument that STAT-1 acts as a tumour suppressor.
SRP5142 STAT5, His tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5143 STAT6, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP2106 TATA box binding protein,GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE) The TATA-binding protein (TBP) is believed to function as an essential factor of the general transcription machinery and to be involved in transcription by all three eukaryotic RNA polymerases (pol I, II, and III). TBP specifically binds to the TATA element at the promoter region and interacts with numerous transcription factors, including TBP-associated factors (TAFs), activators, and some tumor suppressor proteins.
SRP2003 TBP (TATA box binding protein) human recombinant, expressed in E. coli, ≥85% (SDS-PAGE) TBP (TATA-box binding protein) is essential for the optimal initiation of transcription of ribosomal, messenger, small nuclear, and transfer RNAs by all three eukaryotic RNA polymerases. TBP proteins binds to the TATA consensus sequence (TATAa/tAa/t) with high affinity, through its C-terminal or core region, and identifies minor groove segments and introduces significant DNA deformation. It is a component of the class II initiation factor TFIID, along with TBP-associated factors (TAFIIs), which is crucial for nucleating the assembly of Pol II pre-initiation complex (PIC). PIC is essential for the transcription initiation by RNA polymerase II (Pol II). Amplification of the CAG/CAA trinucleotide repeats in TBP gene results in an autosomal dominant cerebellar ataxia, SCA17 (spinocerebellar ataxia type 17), which is characterized by ataxia, dystonia, parkinsonism, and chorea.
The TATA-binding protein (TBP) is believed to function as an essential factor of the general transcription machinery and to be involved in transcription by all three eukaryotic RNA polymerases (pol I, II, and III). TBP specifically binds to TATA element at the promoter region and interacts with numerous transcription factors, including TBP-associated factors (TAFs), activators, and some tumor suppressor proteins.
SRP2002 TFIIA-p12 human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) p12 is a small subunit ( γ ) of the transcription factor IIA and has been shown to be required for both basal and activated transcription. Recombinant p12, along with two other subunits ( α and β ) can potentiate transcriptional activation, whereas p12 along with β subunit is able to function in an anti-repression for reconstitued TFIIA, containing all three subunits.
SRP2111 TFIIA (p12), γ subunit, GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE) p12 is a small subunit γ of the transcription factor IIA and has been shown to be required for both basal and activated transcription. Recombinant p12, along with two other subunits (α and β) can potentiate transcriptional activation, whereas p12 along with a β subunit is able to function in an anti-repression.
SRP2001 TFIIA-p55 human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) The transcription factor IIA (TFIIA) has been shown to bind to the TBP-DNA complex and to increase the affinity of TBP for the TATA element. Human TFIIA consists of three subunits of 35 kDa (a subunit), 19 kDa (b subunit) and 12 kDa (g subunit). The a and b subunits are derived from the product, p55, of a single gene by an unknown mechanism. However, recombinant p55, in combination with a 12 kDa subunit (g subunit), retains native TFIIA activity for reconstituted TFIIA, containing all three subunits.
SRP2028 TFIIA, reconstituted human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) The transcription factor IIA (TFIIA) has been shown to bind to the TBP-DNA complex and to increase the affinity of TBP for the TATA element. Human TFIIA consists of three subunits of 35 kDa (α subunit), 19 kDa (β subunit) and 12 kDa (γ subunit). The α and β subunits are derived from the product, p55, of a single gene by an unknown mechanism. However, recombinant p55, in combination with a 12 kDa subunit (γ subunit), retains native TFIIA activity.
T8819 TFIIB human ~5 units/μL, recombinant, expressed in E. coli, solution General transcription factor for RNA Polymerase II.
The amino terminal region of TFIIB contains a zinc ribbon fold composed of antiparallel Β strands. Mutational studies show that this domain is required for recruitment of RNA Pol II for transcriptional initiation.
SRP2112 TFIIB, GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE) The transcription factor IIB (TFIIB) is an essential factor for transcription by RNA polymerase II. TFIIB has been shown to be required for selective binding of RNA polymerase II, TFIIF and TFIID-DNA complex, and for specifying the start site of transcription. Human TFIIB is a single, 35 kDa polypeptide, homologous to yeast factor, the product of the SUA7 gene.
SRP2012 TFIID, native complex human ≥70% (SDS-PAGE) TFIID is a multiprotein complex with a molecular mass of around 750 kDa that directs pre-initiation complex assembly on both TATA box-containing and TATA-less promoters. It consists of TATA-binding protein (TBP) and a number of TBP associated factors (TAFs). TBP alone can replace TFIID in a reconstituted in vitro transcription system but only the TFIID complex can mediate transcriptional activation. TAFII250, the largest subunit of TFIID contains protein kinase and histone acetyltransferase activities linking transcriptional initiation/activation with chromatin modification. In addition, multiple serine/ threonine phosphorylations of TBP and TAFs selectively inhibit the ability of TFIID to mediate transcriptional activation.
SRP2005 TFIIE β, p34 human recombinant, expressed in E. coli, ≥70% (SDS-PAGE) The human Transcription Factor IIE (TFIIE) is composed of 56 kDa ( α) and 34 kDa ( β) subunits and is shown to be a heterotetramer. The 56-kDa subunit contains a region similar to a zinc-binding domain and a region sharing homology with the catalytic loop of a kinase domain. TFIIE binds to RNA polymerase II in solution and joins the pre-initiation complex probably concomitant with RNA polymerase II and TFIIF.
SRP2004 TFIIE α, p56 human recombinant, expressed in E. coli, ≥70% (SDS-PAGE) The human Transcription Factor IIE (TFIIE) is composed of 56 kDa ( α) and 34 kDa ( β) subunits and is shown to be a heterotetramer. The 56-kDa subunit contains a region similar to a zinc-binding domain and a region sharing homology with the catalytic loop of a kinase domain. TFIIE binds to RNA polymerase II in solution and joins the pre-initiation complex probably concomitant with RNA polymerase II and TFIIF.
SRP2113 TFIIE, α (p56), α subunit, GST tagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) The human Transcription Factor IIE (TFIIE) is composed of 56 kDa and 34 kDa subunits and is shown to be a heterotetramer. The 56- kDa subunit contains a region similar to a zinc-binding domain and a region sharing homology with the catalytic loop of a kinase domain. TFIIE binds to RNA polymerase II in solution and joins the preinitiation complex probably concomitant with RNA polymerase II and TFIIF.
SRP2006 TFIIE, α+β subunits human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) The human Transcription Factor IIE (TFIIE) is composed of 56 kDa (α) and 34 kDa (β) subunits and is shown to be a heterotetramer. The 56 kDa subunit contains a region similar to a zinc-binding domain and a region sharing homology with the catalytic loop of a kinase domain. TFIIE binds to RNA polymerase II in solution and joins the pre-initiation complex probably concomitant with RNA polymerase II and TFIIF.
SRP2009 TFIIF (RAP30+Rap74) human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) The transcription factor IIF (TFIIF) is composed of 58 kDa (RAP74) and 26 kDa (RAP34) subunits as a heterodimer, and was first identified through the ability to interact with immobilized RNA polymerase II. The Rap74 subunit of TFIIF can be phosphorylated by TAF250 both in vivo and in vitro. The RAP30 subunit of TFIIF contains two distinct regions with sequence similarity to E. coli s factors and can deliver RNA polymerase II to the promoter to support transcription initiation in the absence of RAP74.
SRP2008 TFIIF (RAP30 subunit) human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) The transcription factor IIF (TFIIF) is composed of 58 kDa (RAP74) and 26 kDa (RAP30) subunits that form a heterodimer, and was first identified through the ability to interact with immobilized RNA polymerase II. The RAP30 subunit of TFIIF contains two distinct regions with sequence similarity to E. coli factors and can deliver RNA polymerase II to the promoter to support transcription initiation in the absence of RAP74.
SRP2114 TFIIF, Rap30 subunit, GST tagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) The transcription factor IIF (TFIIF) is composed of 58 kDa (RAP74) and 26 kDa (RAP30) subunits as a heterodimer, and was first identified through the ability to interact with immobilized RNA polymerase II. The RAP30 subunit of TFIIF contains two distinct regions with sequence similarity to E coli factors and can deliver RNA polymerase II to the promoter to support transcription initiation in the absence of RAP74.
SRP2007 TFIIF (RAP74 subunit) human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) The transcription factor IIF (TFIIF) is composed of 58 kDa (RAP74) and 26 kDa (RAP30) subunits that form a heterodimer, and was first identified through the ability to interact with immobilized RNA polymerase II. In addition to its role in transcription initiation, TFIIF can increase the specificity and efficiency of RNA polymerase II transcription, and can especially increase the rate of transcription elongation.
SRP2010 TFIIH, native complex human ≥75% (SDS-PAGE) TFIIH is a multicomponent basal transcription factor complex. Nine subunits have been identified within the TFIIH holoenzyme complex. Various enzymatic activities, including DNA repair, helicase, and cyclin-dependent kinase activities, have been reported. The XPB, p62, p52, p44, and p34 subunits are thought to constitute the "core" of the TFIIH transcription machinery. Although the p44 and p34 subunits have no defined enzymatic activity, their zinc finger structures suggest that they may be DNA-binding proteins that might mediate interactions with soluble transcription factors. The cdk-activating kinase (CAK) subcomplex, comprising subunits Cdk7, cyclin H, amd MAT1, phosphorylate several cyclin-dependent kinases (cdks), as well as the carboxy-terminal domain of pol II. Several inherited human disorders such as Xeroderma pigmentosum (XP), Cockayne syndrome (CS) and trichothiodystrophy (TTD) are associated with mutations in TFIIH subunits.
SRP2011 TFIIH, p62 subunit human recombinant, expressed in E. coli, ≥70% (SDS-PAGE) TFIIH, a multi-subunit complex is involved in several biological fundamental mechanisms of the cell: transcription, nucleotide excision repair and cell cycle regulation. p62 is one of the six subunits that constitutes the core of TFIIH. Analysis of the expression of the p62 gene reveals an over-expression in testis tissue. This subunit of TFIIH participates in a variety of protein-protein interactions. For example, Rb competes with TBP and p62 for binding to E2F thus repressing E2F-mediated trans-activation; herpes simplex virus VP16 and human p53 directly interact with the p62 subunit of TFIIH. In addition, TFIIH, via p62 phosphorylation is the major target for mitotic inactivation of transcription.
SRP2102 TNFα, low endotoxin, His tagged human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Tumor necrosis factor α (TNFα or TNFSF2) is produced by many different cell types including activated monocytes, fibroblasts, endothelial cells, macrophages, T-cells, B-lymphocytes, granulocytes, smooth muscle cells, eosinophilis, chondrocytes and other cell types. It functions as a cytokine involved in cell proliferation, differentiation, apoptosis, lipid metabolism and coagulation. High level of TNFα leads to the development of inflammatory responses that are hallmarks of many diseases including autoimmune diseases, insulin resistance and cancer. The active form of TNFα (18 kDa) is generated by the cleavage of an Ala-Val bond between residues 76-77 of the precursor protein.
SRP2033 Topo I (197-651) (core domain) human recombinant, expressed in insect cells, ≥80% (SDS-PAGE) Human DNA topoisomerase I is the best studied of the DNA topoisomerase family. It catalyzes the relaxation of both positive and negative supercoils without the requirement of energy. In addition to DNA replication and transcriptional activation, DNA topoisomerase I also plays a major role in pre-mRNA splicing, cell cycle and other gene regulatory pathways during cell growth and development. The core domain spanning from amino acids 215 to 636 is highly conserved and retains DNA binding activity. Topo I has been found to nick the DNA with a preference of 5’-(A/T)(G/C)(A/T)T-3’. Camptothecin and its analogs have been tested as potent anticancer compounds by stabilizing topo I-DNA complex, thereby inhibiting both DNA and RNA synthesis.
SRP2032 Topo I (C651-765) (C terminal domain) human recombinant, expressed in insect cells, ≥80% (SDS-PAGE) Human DNA topoisomerase I catalyzes the relaxation of both positive and negative supercoils without the requirement of energy. In addition to DNA replication and transcriptional activation, DNA topoisomerase I also plays a major role in pre-mRNA splicing, recombination, chromatin remodeling and other DNA or RNA templating activities. The C terminal domain of DNA topoisomerase I spanning from amino acids 713 to 765 is highly conserved and connected to the core domain by a poorly conserved linker domain (residues 636-713). An active site tyrosine has been characterized at position 723. Mutation of this tyrosine to phenylalanine at position 723 causes topo I to preferentially bind the supercoiled DNA rather than relaxed DNA in the mixture of supercoiled and relaxed DNA.
SRP2034 Topo I (N1-197) (NTD) human recombinant, expressed in insect cells, ≥85% (SDS-PAGE) Human DNA topoisomerase I is the best studied of the DNA topoisomerase family. It catalyzes the relaxation of both positive and negative supercoils without the requirement of energy. In addition to DNA replication and transcriptional activation, DNA topoisomerase I also plays a major role in pre-mRNA splicing, cell cycle and other gene regulatory pathways during cell growth and development. The N-terminal 214 amino acids of topoisomerase I comprise a highly charged N-terminal domain (NTD) involved in protein-protein interactions with a number of cellular proteins, including SV40 T antigen, nucleolin, SR proteins, p53 and other transcription factors.
SRP2035 Topo I (Y723F) (mt Y723F) human recombinant, expressed in insect cells, ≥80% (SDS-PAGE) Human DNA topoisomerase I is the best studied of the DNA topoisomerase family. It catalyzes the relaxation of both positive and negative supercoiled DNAs without the requirement of energy. In addition to DNA replication and transcriptional activation, DNA topoisomerase I also plays a major role in pre-mRNA splicing, cell cycle and other gene regulatory pathways during cell growth and development. Tyrosine 723 was identified as an active site for the DNA binding activity of DNA topoisomerase I. The covalent intermediate of topo I and DNA complex includes nucleophilic attack by the O4-oxygen of tyrosine 723 on a phosphester linkage in the DNA. Mutation from tyrosine to phenylalanine at position 723 preferentially binds the supercoiled DNA rather than relaxed DNA in the mixture of supercoiled and relaxed DNAs. But mutation at tyr723 neither affects its kinase activity that phosphorylates splicing factors of SR protein family nor its transcription activity of class II genes in vitro.
SRP0481 TRIM24 (896-1014) human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)  
SRP2053 USF1 human recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Human Upstream Stimulatory Factor 1 (USF1) regulates the transcription of many genes involved in lipid and glucose homeostasis and co-localizes with familial combined hyperlipidemia (FCHL) and type 2 diabetes on chromosome 1q22-23. The USF1 protein can activate transcription through pyrimidine-rich initiator (Inr) elements and E-box motifs. It is a basic helix-loop-helix leucine zipper (b-HLH-ZIP) protein that shares a common DNA-binding specificity with the c-Myc oncoproteins.
SRP2084 VHL human recombinant, expressed in insect cells, ≥70% (SDS-PAGE) von Hippel-Lindau (VHL) disease is a hereditary cancer with a predilection for the central nervous system and retina. The von Hippel-Lindau tumor suppressor gene is mutated in families with von Hippel-Lindau disease and encodes a protein (VHL) of 213 amino acids with an acidic pentapeptide motif in the N-terminus. Mutations in the VHL gene result in constitutive expression of many hypoxia-induced genes, at least in part because of increases in the cellular level of hypoxia-inducible transcription factor HIF-1a. VHL protein binds to elongin B, elongin C, and Cul2 to form a stable complex that targets hypoxia inducible factors (HIFs) for degradation and transcriptional regulation. In addition, VHL protein has also been shown to interact with specific protein kinase C isoforms, histone deacetylases and HIF-1 inhibitor (HIF-1).
SRP2074 Vitamin D receptor (118-427), His tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE) The vitamin D endocrine system is critical for the proper development and maintenance of mineral ion homeostasis and skeletal integrity. Beyond these classical roles, recent evidence suggests that the bioactive metabolite of vitamin D, 1,25-dihydroxyvitamin D3, functions in diverse physiological processes, such as hair follicle cycling, blood pressure regulation, and mammary gland development. The biological effects of 1,25-(OH)2D3 are mediated through the vitamin D receptor (VDR), a member of the nuclear receptor superfamily of ligand-activated transcription factors. The cellular effects of VDR signaling include growth arrest, differentiation and/or induction of apoptosis. VDR heterodimerizes with RXR and the liganded VDR-RXR heterodimer binds with high affinity to vitamin D response elements (VDREs) in the promoters of target genes. In addition, several nuclear receptor coactivators (SRC-1, DRIP) have been shown to interact with VDR and potentiate its transcriptional activity. In addition to treating disorders of mineral metabolism and diseases of the skeleton, such as rickets, osteoporosis, and renal osteodystrophy, VDR and 1,25-(OH)2D3 have significant therapeutic potential for pathologies such as cancer, autoimmune syndromes, and psoriasis.
SRP2121 VP16 (411-490), GST tagged from human herpesvirus 2 recombinant, expressed in E. coli, ≥80% (SDS-PAGE) Herpes virus VP16 activates expression of immediate early genes in virally-infected cells. As most other eukaryotic transcriptional activator proteins, VP16 has a modular domain structure: its N-terminus is involved in DNA-protein interactions, while its C-terminal 79 amino acids have proven to be an especially potent transactivation domain. VP16 has been shown to bind to TBP, TFIIB, and replication factor A.
The protein activates the lytic cycle of the virus. It has been shown to have a role in viral assembly and maturation.
SAB4200464 Monoclonal Anti-WDR37 antibody produced in mouse ~1.0 mg/mL, clone WDR37-9, purified immunoglobulin  
SRP2082 WT-1 (+KTS) human recombinant, expressed in insect cells, ≥60% (SDS-PAGE) WT-1, the product of Wilms’ tumor suppressor gene Wt1, is a nuclear protein with structural motifs characteristic of transcription factors, including four C-terminal zinc fingers. While different pre-mRNA processing could result in 16 isoforms of the protein, the inclusion or exclusion of exon 5 and three amino acids (KTS) between zinc fingers 3 and 4 largely affects the activity of the WT1 protein. Such a complex post-transcriptional regulation, particularly in splicing, may represent a major regulatory mechanism for tumorigenesis of the Wilms’ tumor. With the inclusion of exon 5, WT1 (KTS+) binds to both DNA and RNA and is RNase but not DNase sensitive. This form also co-localizes with splicing factors in a speckled nuclear particle, suggesting that the WT1 protein may function as both a transcription factor and a splicing regulator.
SRP2083 WT-1 (-KTS) human recombinant, expressed in insect cells, ≥60% (SDS-PAGE) WT-1, the product of Wilms’ tumor suppressor gene Wt1, is a nuclear protein with structural motifs characteristic of transcription factors, including four C-terminal zinc fingers. While different pre-mRNA processing could result in 16 isoforms of the protein, inclusion or exclusion of exon 5 and the three amino acids (KTS) between zinc fingers 3 and 4 largely affects the activity of WT1 protein. Such a complex post-transcriptional regulation, particularly in splicing, may represent a major regulatory mechanism for tumorigenesis of the Wilms’ tumor. WT1 (-KTS) appears to have different binding affinity to both DNA and RNA compared to the +KTS form.