Description
Human HEPH Recombinant Protein (N-His)
Human HEPH Recombinant Protein (N-His) is a recombinant protein expressed in E. coli, spanning Ala24-Cys366, with an N-terminal His tag. Predicted molecular weight: 40.65 kDa. Purity: >90% as determined by SDS-PAGE. Supplied lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Applications: ELISA, immunogen, SDS-PAGE and Western blot. Hephaestin is a ~130 kDa protein. Plasma membrane ferroxidase that mediates the extracellular conversion of ferrous/Fe(2+) iron into its ferric/Fe(3+) form. For research use only.
Couples ferroportin which specifically exports ferrous/Fe(2+) iron from cells to transferrin that only binds and shuttles extracellular ferric/Fe(3+) iron throughout the body. By helping iron transfer from cells to blood mainly contributes to dietary iron absorption by the intestinal epithelium and more generally regulates iron levels in the body.
| Product Name: | Human HEPH Recombinant Protein (N-His) |
| SKU: | GXRP02801 |
| Size: | 50 µg, 100 µg, 1 mg |
| Species: | Human |
| Synonyms: | HEPH, KIAA0698, Hephaestin |
| Tag: | N-His |
| Expression Host: | E. coli |
| Protein Length: | Ala24-Cys366 |
| Calculated MW: | 40.65 kDa |
| UniProt: | Q9BQS7 |
| Applications: | ELISA, Immunogen, SDS-PAGE, WB |
| Purity: | >90% as determined by SDS-PAGE. |
| Form: | Lyophilized |
| Formulation: | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1 mM EDTA, 4% Trehalose, 1% Mannitol. |
| Reconstitution: | Reconstitute in sterile water for a stock solution. Adjust the volume of sterile water so that, after reconstitution, the final stock concentration matches the value indicated on the product label or datasheet. |
| Storage: | Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Shipping: | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Note: | For research use only. |