Description
Human EHD1 Recombinant Protein (N-His)
Human EHD1 Recombinant Protein (N-His) is a recombinant protein expressed in E. coli, spanning Thr20-Ser402, with an N-terminal His tag. Predicted molecular weight: 46.23 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. EH domain-containing protein 1 (EHD1) is a ~60 kDa protein. ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. For research use only.
In vitro causes vesiculation of endocytic membranes. Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Recruited to endosomal membranes upon nerve growth factor stimulation, indirectly regulates neurite outgrowth. Plays a role in myoblast fusion.
| Product Name: | Human EHD1 Recombinant Protein (N-His) |
| SKU: | GXRP04526 |
| Size: | 50 µg, 100 µg, 1 mg |
| Species: | Human |
| Synonyms: | PAST, EHD1, PAST1, PAST homolog 1, EH domain-containing protein 1, Testilin, hPAST1 |
| Tag: | N-His |
| Expression Host: | E. coli |
| Protein Length: | Thr20-Ser402 |
| Calculated MW: | 46.23 kDa |
| UniProt: | Q9H4M9 |
| 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. |
