HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.
Greater than 95.0% as determined by SDS-PAGE.
HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa.
The HB-EGF is purified by proprietary chromatographic techniques.
Heparin-binding EGF-like growth factor (HB-EGF) is a member of the EGF family that binds to the EGF receptor, leading to the stimulation of cell proliferation in a variety of cell types including smooth muscle cells, fibroblasts, epithelial cells, and keratinocytes. HB-EGF is found in several cell types and tissues, including vascular endothelial cells, smooth muscle cells, macrophages, skeletal muscle, keratinocytes, and certain tumor cells. Unlike other EGF-like molecules, HB-EGF possesses the unique ability to bind to heparin sulfate proteoglycans, which may contribute to its enhanced mitogenic activity on smooth muscle cells compared to EGF.
Recombinant human HB-EGF, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 87 amino acids with a molecular weight of 9.9 kDa.
Purification of HB-EGF is achieved through proprietary chromatographic techniques.
The protein was lyophilized from a solution containing 10 mM sodium phosphate (pH 7.5) at a concentration of 1 mg/ml.
The purity of the product is determined using SDS-PAGE analysis and is greater than 95.0%.
The biological activity of HB-EGF is measured by its ability to stimulate the proliferation of 3T3 cells. The ED50, defined as the concentration required to induce a half-maximal proliferative response, is in the range of 0.13-0.2 ng/ml. This corresponds to an estimated specific activity of 7.7 x 106 units/mg.
HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.
HB-EGF is synthesized as a precursor protein that undergoes ectodomain shedding to produce the soluble mature form . This mature form influences the mitogenicity and chemotactic factors for smooth muscle cells and fibroblasts . HB-EGF binds to and activates EGFR and ErbB4, leading to the formation of homo- and heterodimers, autophosphorylation of specific tyrosine residues, and subsequent intracellular signaling .
HB-EGF plays a crucial role in various physiological and pathological processes:
Recombinant HB-EGF is produced using expression systems such as baculovirus-infected insect cells . The recombinant protein is used in research to study its biological functions and potential therapeutic applications. It is available in different formulations, including carrier-free versions for specific applications .
Recombinant HB-EGF has several applications in research and medicine: