Target | |
---|---|
Synonyms | Diphtheria toxin receptor;DTR;EGFL;heparin-binding EGF-like growth factor;DTS;DTSF;heparin-binding epidermal growth factor;proheparin-binding EGF-like growth factor;HB-EGF;pro HB-EGF |
Description | Recombinant Human Heparin Binding EGF like Growth Factor is produced by our Mammalian expression system and the target gene encoding Leu20-Leu148 is expressed with a 6His tag at the C-terminus. |
Delivery | In Stock |
Uniprot ID | Q99075 |
Expression Host | HEK293 |
Tag | C-6×His Tag |
Molecular Characterization | Not available |
Molecular Weight | 15.1 KDa |
Purity | Greater than 95% as determined by reducing SDS-PAGE. |
Formulation & Reconstitution | Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4. |
Storage & Shipping | Store at -20°C to -80°C for 12 months in lyophilized form. After reconstitution, if not intended for use within a month, aliquot and store at -80°C (Avoid repeated freezing and thawing). Lyophilized proteins are shipped at ambient temperature. |
Background | Heparin-binding EGF-like growth factor (HB-EGF) is a 12-16 kDa member of the epidermal growth factor (EGF) family. It possesses an EGF-like domain, and a heparin-binding motif. Mature HB-EGF is a soluble peptide that arises from proteolytic processing of the transmembrane form. Human HB-EGF shows 76% and 73% aa sequence identity with rat and mouse HB-EGF, respectively. It is required for normal cardiac valve formation and normal heart function, promotes smooth muscle cell proliferation. It may be involved in macrophage-mediated cellular proliferation; it is mitogenic for fibroblasts, but not endothelial cells. HB-EGF classified as a group 2 ErbB ligand based on its ability to activate both the EGF/ErbB1 and ErbB4 receptors. Activity associated with ErbB4 binding appears to be limited to non-mitogenic actions, while EGFR binding induces both mitogenic and non-mitogenic activity. |
Usage | Research use only |
Human proHB-EGF (C-6His) Protein
Price: 10 μg ¥400.00 ; 50 μg ¥920.00
Product Data
图片
Figure 1. Greater than 95% as determined by reducing SDS-PAGE.
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