

| Catalog No. | HD441012 |
|---|---|
| Description |
Recombinant Human PEPD Protein, N-His (HD441012) expressed in E. coli, spanning Thr188-Lys493. Purity: >90% by SDS-PAGE.
Highlights
|
| Expression system | E. coli |
| Accession | P12955 |
| Protein length | Thr188-Lys493 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Homo sapiens (Human) |
| Nature | Recombinant |
| Endotoxin level | Please contact with the lab for this information. |
| Purity | >90% as determined by SDS-PAGE. |
| Predicted molecular weight | 36.09 kDa |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Alternate Names | EC:3.4.13.9, Imidodipeptidase, PEPD, PRD, Peptidase D, Prolidase, Proline dipeptidase, X-Pro dipeptidase, Xaa-Pro dipeptidase |
| Background | Xaa-Pro dipeptidase is a ~54 kDa protein. Dipeptidase that catalyzes the hydrolysis of dipeptides with a prolyl (Xaa-Pro) or hydroxyprolyl residue in the C-terminal position. The preferred dipeptide substrate is Gly-Pro, but other Xaa-Pro dipeptides, such as Ala-Pro, Met-Pro, Phe-Pro, Val-Pro and Leu-Pro, can be cleaved. Plays an important role in collagen metabolism because the high level of iminoacids in collagen. 1. Lupi, A. et al. (2006) The FEBS journal 273, 5466-78. PMID: 17081196 2. Rao, SD. et al. (2022) Nature chemical biology 18, 565-574. PMID: 35165443 3. Endo, F. et al. (1989) The Journal of biological chemistry 264, 4476-81. PMID: 2925654 |
| Note | For research use only |
Contact us for custom quotes, bulk requests and any other issues.
Mail: [email protected]
+86-27-65523339
Building C, No. 666, Shen Dun Si Lu, Wuhan, 430206, China
中文
English
한국어
日本語
Español
Français
Русский