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Human TGF-α Recombinant Protein
Cytokines & Growth Factors
Growth Factors and Cytokines

Human TGF-α Recombinant Protein #44909

Citations (0)
Serial dilutions of Human TGF-α Recombinant Protein were added to Balb/c-3T3 cells. Cell proliferation was measured and the linear portion of the curve was used to calculate the ED50.
The purity of Human TGF-α Recombinant Protein was determined by SDS-PAGE of 1 µg reduced (+) and non-reduced (-) recombinant hTGF-α and staining with Coomassie Blue.


Human TGF-α Recombinant Protein is supplied as lyophilized material that is very stable at -20°C. It is recommended to reconstitute with sterile water at a concentration of 0.1 mg/ml which can be further diluted in aqueous solutions as needed. Addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage.

Once in solution, store at 4°C and use within 1 month, or store at -20ºC to -80ºC and use within 3 months to prevent loss of potency. Aliquot to avoid multiple freeze/thaw cycles if storing reconstituted material at -20ºC to -80ºC.

Product Description

MW (kDa) 5.6
Purity A greater than or equal to 95% purity was determined by SDS-PAGE.
Endotoxin Endotoxin levels are less than or equal to 1 EU / 1 μg hTGF-α.
Activity 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.

Source / Purification

Recombinant human TGF-α was expressed in Balb/c-3T3 cells and is supplied in a lyophilized form.


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).


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Limited Uses

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For Research Use Only. Not for Use in Diagnostic Procedures.
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To Purchase # 44909
Cat. # Size Qty. Price
25 µg