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Merck

T7039

Transforming Growth Factor-β1 human

≥98% (SDS-PAGE), recombinant, expressed in CHO cells, powder, suitable for cell culture

Synonym(s):

hTGF-β1, TGF-β1

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.77
MDL number:

Product Name

Transforming Growth Factor-β1 human, TGF-β1, recombinant, expressed in CHO cells, powder, suitable for cell culture

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

technique(s)

cell culture | mammalian: suitable

impurities

<1 EU/μg

UniProt accession no.

storage temp.

−20°C

Quality Level

Gene Information

human ... TGFB1(7040)

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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.

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.

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.

Physical form

Lyophilized from a 0.2 μm filtered aqueous solution.

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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)
Louis A Saddic et al.
Cardiovascular diabetology, 16(1), 87-87 (2017-07-09)
Omentin-1, also known as Intelectin-1 (ITLN1), is an adipokine with plasma levels associated with diabetes, obesity, and coronary artery disease. Recent studies suggest that ITLN1 can mitigate myocardial ischemic injury but the expression of ITLN1 in the heart itself has
Transforming Growth Factor-β Induces Renal Epithelial
Jagged-1 Expression in Fibrotic Disease
Morrissey J, et al.
Journal of the American Society of Nephrology, 13, 1499- 1508 (2002)
TGF β signalling and its role in tumour pathogenesis.
Kaminska B, et al.
Acta Biochimica Polonica, 52(2), 329-337 (2005)

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