5.6
#P01135
7039
Background
Transforming growth factor alpha (TGF-alpha) is a member of the epidermal growth factor (EGF) family, sharing the same receptor, EGFR, and regulating cell proliferation, survival, and differentiation (1). Members of the family share an EGF-like domain of 45-60 amino acids characterized by the conservation of six regularly spaced cysteines, forming three disulfide bonds that function as their receptor binding domain. TGF-alpha was initially discovered in the media of retrovirally transformed fibroblasts, and its name comes from its ability to induce transformation in cultured fibroblasts (2). This transforming activity was later shown to require TGF-beta, which potentiates the activity of TGF-alpha through a separate receptor (3). Soluble TGF-alpha is released from its membrane-bound precursor, pro-TGF-alpha, following protolytic cleavage, but the membrane bound precursor is still able to bind and activate EGFR (4). Binding of soluble or membrane bound TGF-alpha to EGFR leads to receptor dimerization, tyrosine autophosphorylation, and activation of downstream signaling components. TGF-alpha and related peptides play an important role in the progression of cancer as well as in neuropathological processes (5,6).
- Derynck, R. (1986) J Cell Biochem 32, 293-304.
- de Larco, J.E. and Todaro, G.J. (1978) Proc Natl Acad Sci U S A 75, 4001-5.
- Roberts, A.B. et al. (1981) Proc Natl Acad Sci U S A 78, 5339-43.
- Wong, S.T. et al. (1989) Cell 56, 495-506.
- Rusch, V. et al. (1996) Cytokine Growth Factor Rev 7, 133-41.
- Junier, M.P. (2000) Prog Neurobiol 62, 443-73.
Endotoxin
Endotoxin levels are less than or equal to 1 EU / 1 μg hTGF-α.
Purity
A greater than or equal to 95% purity was determined by SDS-PAGE.
Source / Purification
Recombinant human TGF-α was expressed in Balb/c-3T3 cells and is supplied in a lyophilized form.
Bioactivity
The bioactivity of recombinant hTGF-α was determined in a Balb/c-3T3 cell proliferation assay. The ED50 of each lot is less than or equal to 2 ng/ml.
Background
Transforming growth factor alpha (TGF-alpha) is a member of the epidermal growth factor (EGF) family, sharing the same receptor, EGFR, and regulating cell proliferation, survival, and differentiation (1). Members of the family share an EGF-like domain of 45-60 amino acids characterized by the conservation of six regularly spaced cysteines, forming three disulfide bonds that function as their receptor binding domain. TGF-alpha was initially discovered in the media of retrovirally transformed fibroblasts, and its name comes from its ability to induce transformation in cultured fibroblasts (2). This transforming activity was later shown to require TGF-beta, which potentiates the activity of TGF-alpha through a separate receptor (3). Soluble TGF-alpha is released from its membrane-bound precursor, pro-TGF-alpha, following protolytic cleavage, but the membrane bound precursor is still able to bind and activate EGFR (4). Binding of soluble or membrane bound TGF-alpha to EGFR leads to receptor dimerization, tyrosine autophosphorylation, and activation of downstream signaling components. TGF-alpha and related peptides play an important role in the progression of cancer as well as in neuropathological processes (5,6).
Background References
Cross-Reactivity Key
H: human M: mouse R: rat Hm: hamster Mk: monkey Vir: virus Mi: mink C: chicken Dm: D. melanogaster X: Xenopus Z: zebrafish B: bovine Dg: dog Pg: pig Sc: S. cerevisiae Ce: C. elegans Hr: horse GP: Guinea Pig Rab: rabbit All: all species expected
Trademarks and Patents
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