| Target | |
|---|---|
| Synonyms | Diphtheria toxin receptor; DTR;HEGFL; 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-6His tag |
| Molecular Characterization | #N/A |
| 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 | Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.Reconstituted protein solution can be stored at 4-7°C for 2-7 days.Aliquots of reconstituted samples are stable at < -20°C for 3 months. |
| Usage | Research use only |
| Background | Heparin-binding EGF-like growth factor (HB-EGF) is a 1216 kDa member of the epidermal growth factor (EGF) family. It possesses an EGFlike domain, and a heparin-binding motif. Mature HBEGF is a soluble peptide that arises from proteolytic processing of the transmembrane form. Human HBEGF shows 76% and 73% aa sequence identity with rat and mouse HBEGF, 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. HBEGF 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 nonmitogenic actions, while EGFR binding induces both mitogenic and nonmitogenic activity. |
Human proHB-EGF (C-6His) Protein
Price: 50 μg $131.00
Product Data
Images
Figure 1. Greater than 95% as determined by reducing SDS-PAGE.