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T7039

Sigma-Aldrich

Transforming Growth Factor-β1 human

TGF-β1, recombinant, expressed in CHO cells, powder, suitable for cell culture

Synonym(s):
TGF-β1, hTGF-β1
MDL number:
NACRES:
NA.77

Quality Level

biological source

human

recombinant

expressed in CHO cells

assay

≥98% (SDS-PAGE)

form

powder

potency

≤0.05 ng/mL ED50

quality

endotoxin tested

mol wt

protein 25 kDa

packaging

pkg of 2 μg
pkg of 50 μg

storage condition

avoid repeated freeze/thaw cycles

application(s)

cell culture | mammalian: suitable

impurities

<1 EU/μg

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... TGFB1(7040)

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General description

Tgfb1 (transforming growth factor-β1 human) is a 25kDa peptide encoded by the gene mapped to human chromosome 19q13.2. TGF-β1 polypeptide is produced as a precursor with hydrophobic signal sequence, pro-region and mature peptide. Cleavage of the precursor at tetrabasic cleavage site results in monomers of carboxy-terminal 112 amino acids. The biologically active form of Tgfb1 exists as a disulphide-linked homodimer. In mammals, three isoforms of TGF-β has been identified : TGF-β1, TGF-β2 and TGF-β3.

Application

Transforming Growth Factor-β1 human has been used in
  • reporter gene assay.
  • in vitro transfection.
  • to study the effect of transforming growth factor-β1 (TGF-β1) on gene array analysis of renal cells.
  • to study the association of TGF-β1 with shear stress-dependent upregulation of tissue inhibitor of metalloproteinase-1 in microvascular endothelial cells.
  • to study the interaction between TGF-β1 activation and myofibroblast formation.

Biochem/physiol Actions

TGF-β1 is a multifunctional peptide capable of influencing cell proliferation, tissue growth, differentiation, and other functions in a wide range of cell types. TGF-β1 plays a fundamental role in differentiation by involvement in adipogenesis, myogenesis, chondrogenesis, osteogenesis, epithelial cell differentiation and immune cell function. All cells possess a specific TGF-β1 receptor. Both transformed and non-neoplastic tissues release transforming growth factors.The multi-modal nature of TGF-β1 is seen in its ability to stimulate or inhibit cellular proliferation. TGF-β1 is associated with the developmental and metastasis of colorectal cancer.
Transforming growth factor-β1 (TGF-β1) is produced by many cell types, but is reported to be most concentrated in mammalian platelets, where it is present at approximately four times the level of TGF-β2.

Physical form

Lyophilized from a 0.2 μm filtered aqueous solution.

Analysis Note

The biological activity of TGF-β1 is measured in culture by inhibition of mouse IL-4-dependent proliferation of mouse HT-2 cells.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

Certificate of Analysis

Certificate of Origin

Liang Zhang et al.
FEBS letters, 584(22), 4646-4654 (2010-10-26)
Epithelial-to-mesenchymal transition (EMT) has been implicated in various physiological and pathological events. In this study, we found that the synthetic glucocorticoid dexamethasone (Dex) can inhibit transforming growth factor-beta1-induced EMT and cell migration. We also demonstrated that Dex inhibits EMT through...
Interplay between TGF-β signaling and receptor tyrosine kinases in tumor development.
Shi Q and Chen YG
Science China: Life Sciences, 60(10), 1133-1141 (2017)
Matrix metalloproteinase inhibition delays wound healing and blocks latent transforming growth factor-β1 promoted myofibroblast formation and function
Mirastschijski U, et al.
Wound Repair and Regeneration, 18(2), 223-234 (2010)
Endothelial cell TIMP-1 is upregulated by shear stress via Sp-1
and the TGF1 signaling pathways
Uchida C and Haas TL
Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire, 92.1, 77-83 (2013)
Transforming growth factor β and platelet-derived growth factor modulation of myofibroblast development from corneal fibroblasts in vitro
Singh V, et al.
Experimental Eye Research, 120, 152-160 (2014)

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