Calcium-associated Proteins

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C1907 Calcineurin from bovine brain lyophilized powder, ≥2,500 units/mg protein Calcineurin is a cyclosporin-sensitive, calcium-regulated, serine-threonine protein phosphatase with broad substrate specificity. It is the major calmodulin-binding protein found in the brain. First identified as an inhibitor of the calmodulin activation of phosphodiesterase 3′:5′ cyclic nucleotide (PDE), calcineurin has similar effects on adenylate cyclase. Serves as a key enzyme involved in T-cell activation. Also involved in the hyperphosphorylation of tau protein in Alzheimer′s disease and has been shown to prevent calpain-mediated proteolysis of tau in differentiated PC12 cells.
P1431 Calmodulin from bovine testes BioUltra, ≥98% (SDS-PAGE), lyophilized powder Ca2+ binding protein that is required for activation of cyclic nucleotide-dependent phosphodiesterase. It is also a cofactor/activator of nitric oxide synthase, calcineurin, and many kinases including ATPase, myosin light chain kinase, and CAM kinase I, II, and III. It mediates ryanodine receptor activation by cyclic ADP ribose and is involved in intracellular Ca2+ homeostasis.
SRP5169 Calmodulin1, His tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
A6112 Calmodulin-Agarose saline suspension  
C4714 Calreticulin from bovine liver ≥90% (SDS-PAGE), lyophilized powder A high-affinity calcium binding protein which plays a dynamic role in calcium homeostasis. In addition, calreticulin binds directly to the DNA domain of hormone receptors as well as to the regulatory cytoplasmic domain of proteins of the integrin family. Calreticulin has also been shown to possess a chaperone function.
SRP8001 Calreticulin human recombinant, expressed in E. coli, His tagged, >90% (SDS-PAGE) Calreticulin is involved in regulation of intracellular Ca2+ homoeostasis and ER Ca2+ capacity. It constitutes together with calnexin and ERp57 the ′calreticulin/calnexin cycle′ that is responsible for folding and quality control of newly synthesized glycoproteins. Calreticulin has been implicated to play a role in many biological systems, including functions inside and outside the ER, indicating that the protein is a multi-process molecule. Recently, Calreticulin was shown to enhance the merger of macrophages and tumor cells, increasing phagocytosis.
SRP4809 Calretinin from mouse recombinant, expressed in E. coli, ≥90% (SDS-PAGE), ≥90% (HPLC) Calretinin is widely distributed in the brain and might be responsible for neural protection. It regulates calcium signaling in neurons. Absence of calretinin in mice negatively affects long-term potentiation, motor coordination and Purkinje cell activity.
SRP5170 CaMKPase, GST tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5203 LC20, GST tagged from mouse recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP4913 Nesfatin-1 recombinant, expressed in E. coli, ≥95% (SDS-PAGE)  
SRP4914 Nesfatin-1 from rat recombinant, expressed in E. coli, ≥95% (SDS-PAGE)  
SRP3291 NESFATIN-1 human recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC) Nesfatin-1 is a metabolic polypeptide encoded in the N-terminal region of the precursor protein, Nucleobindin2 (NUCB2). Recombinant human Nesfatin-1 is a 9.7 kDa protein containing 82 amino acid residues.
O5761 Osteocalcin fragment 1-49 Human ≥94% (HPLC), solid  
SRP5223 PAD1, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution Peptidyl arginine deiminases catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The overexpression of PAD1 induced a distinctive pattern of multidrug resistance in mammalian cells and moderate resistance to ultraviolet light. PAD1 is also responsible for substrate deubiquitination during proteasomal degradation. It deiminates filaggrin in the last stages of keratinocyte differentiation. Thus, PAD1 has a role in epidermis function and homeostasis. The protein has been genetically associated with rheumatoid arthritis.
SRP5224 PAD2, GST tagged from mouse recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
SRP5225 PAD3, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution Peptidyl arginine deiminases catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. PAD3 modulates hair structural proteins, such as filaggrin in the hair follicle and trichohyalin in the inner root sheath, during hair follicle formation. It converts arginine to citrulline in filaggrin at a faster rate than it does in trichohyalin. Together with the type I enzyme (PAD1), PAD3 play a role in terminal differentiation of the epidermis.
SRP5226 PAD4, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution Peptidyl arginine deiminases (PADIs) are responsible for the post-translational conversion of peptidylarginine to citrulline, in the presence of calcium ions. In individuals with rheumatoid arthritis (RA), this gene is expressed in hematological cells and synovial tissues, and variant in this gene is linked with susceptibility to RA. The expression of this protein is linked with DNA hypermethylation in acute promyelocytic leukemia (APL).
SRP5227 PAD6, GST tagged human recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution Peptidyl arginine deiminases (PADs) convert arginine residues to citrulline residues in the presence of calcium ions. The PAD family members are thought to be involved in multiple sclerosis and rheumatoid arthritis pathophysiology, and they play a role in epidermis homeostasis. PAD6 is essential for formation of a novel oocyte-restricted fibrous structure, the cytoplasmic lattices (CPLs). PAD6/CPL superstructure plays a key role in regulating microtubule-mediated organelle positioning and movement.
SRP5147 Troponin1, His tagged human recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution  
T9924 Troponin I from human heart lyophilized powder The inhibiting subunit of troponin, responsible for preventing actin-myosin binding and ATPase activity.
Troponin I interacts with tropomyosin for regulating the contraction of striated muscle in a calcium-dependent manner. Additionally, Troponin I can also inhibits actomyosin ATPase and serves as a selective and potent inhibitor of angiogenesis in vivo and in vitro and of tumor metastasis in vivo.
T0175 Troponin T from human heart ≥60% (SDS-PAGE), lyophilized powder The tropomyosin-binding subunit of troponin