HB-EGF Background Information Heparin binding epidermal-like growth factor (HB-EGF), a member of the EGF family of mitogens, binds to the EGF receptor (EGFR) and to heparin sulfate proteoglycans on the cell surface. HB-EGF was originally isolated from medium conditioned by the growth of the human histocytic lymphoma cell U-937 on the basis of its heparin-binding ability and its mitogenic activity for Balb-3T3 fibroblasts. The HB-EGF gene encodes a 208 amino acid precursor containing a signal peptide and transmembrane domain. Mature HB-EGF is a soluble protein 86 amino acids in length and results from the enzymatic cleavage of the membrane bound precursor. The membrane-bound form of HB-EGF has been identified as the diphtheria toxin receptor. Preincubation of Vero cells with phorbol 12-myristate 13-acetate (PMA) induces the proteolytic cleavage of HB-EGF outside the membrane anchor.
HB-EGF (M-18) Product Citations
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HB-EGF (M-18)
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HB-EGF (M-18): sc-1414. Western blot analysis of human recombinant HB-EGF.