Heparin-Binding EGF-Like Growth Factor human 

The biological activity is measured by its ability to stimulate ³H-thymidine incorporation in the EGF-responsive BALB/3T3 cells.

Heparin-binding epidermal growth factor (HB-EGF), like BTC, is a heparin-binding EGF family member. Natural soluble HB-EGF is a 19 kDa glycoprotein of multiple forms due to heterogeneous truncations. Soluble HB-EGF is mitogenic and chemotactic for fibroblasts, keratinocytes, and smooth muscle cells but not capillary endothelial cells. Production of HB-EGF is detected in monocytes, macrophages, and vascular and aortic smooth muscle cells (SMC). HB-EGF may play a role in the pathogenesis of atherosclerosis. It may also be an effector of Jun-induced oncogenic transformation. HB-EGF binds to EGFR with high affinity and to ErbB with moderate affinity.

Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline containing 2.5 mg bovine serum albumin.

expressed in Sf21 cells

≥97% (SDS-PAGE and N-terminal analysis)

lyophilized powder

Endotoxin, tested

cell culture tested

human ... HBEGF(1839)

−20°C

Fu, S.L., et al., Heparin-binding epidermal growth factor-like growth factor, a v−Jun target gene, induces oncogenic transformation. Proc. Natl. Acad. Sci. USA 96, 5716, (1999) abstract

Palmer, U., et al., Epidermal growth factor receptor ligands are chemoattractants for normal human mesothelial cells. Eur. Respir. J. 14, 405-411, (1999) abstract

Vinante, F., et al., Granulocyte-macrophage colony-stimulating factor induces expression of heparin-binding epidermal growth factor-like growth factor/diphtheria toxin receptor and sensitivity to diphtheria toxin in human neutrophils. Blood 94, 3169-3177, (1999) abstract

Iwamoto, R., et al., Contact-dependent growth inhibition and apoptosis of epidermal growth factor (EGF) receptor-expressing cells by the membrane-anchored form of heparin-binding EGF-like growth factor. J. Biol. Chem. 274, 25906-25912, (1999) abstract

Elenius, K., et al., Activation of HER4 by heparin-binding EGF-like growth factor stimulates chemotaxis but not proliferation. EMBO J. 16, 1268-1278, (1997) abstract

Lanzrein, M., et al., Diphtheria toxin endocytosis and membrane translocation are dependent on the intact membrane-anchored receptor (HB-EGF precursor) - studies on the cell-associated receptor cleaved by a metalloprotease in phorbol-ester-treated cells. Biochem. J. 310, 285, (1995) abstract

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