

| Catalog No. | HP992022 |
|---|---|
| Description |
Recombinant Human TRAIP Protein, N-GST & C-His (HP992022) expressed in E. coli, spanning Pro2-Asp75. Purity: >90% by SDS-PAGE.
Highlights
|
| Expression system | E. coli |
| Accession | Q9BWF2 |
| Protein length | Pro2-Asp75 |
| 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 | 36.73 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 | E3 ubiquitin-protein ligase TRAIP, EC:2.3.2.27, RING finger protein 206, RNF206, TRAF-interacting protein, TRAIP, TRIP |
| Background | E3 ubiquitin-protein ligase TRAIP is a ~53 kDa protein. E3 ubiquitin ligase required to protect genome stability in response to replication stress. Acts as a key regulator of interstrand cross-link repair, which takes place when both strands of duplex DNA are covalently tethered together, thereby blocking replication and transcription. Controls the choice between the two pathways of replication-coupled interstrand-cross-link repair by mediating ubiquitination of MCM7 subunit of the CMG helicase complex. Short ubiquitin chains on MCM7 promote recruitment of DNA glycosylase NEIL3. If the interstrand cross-link cannot be cleaved by NEIL3, the ubiquitin chains continue to grow on MCM7, promoting the unloading of the CMG helicase complex by the VCP/p97 ATPase, enabling the Fanconi anemia DNA repair pathway. 1. Chapard, C. et al. (2014) Journal of cell science 127, 5149-56. PMID: 25335891 2. Harley, ME. et al. (2016) Nature genetics 48, 36-43. PMID: 26595769 3. Hoffmann, S. et al. (2016) The Journal of cell biology 212, 63-75. PMID: 26711499 4. Soo Lee, N. et al. (2016) Nature communications 7, 10463. PMID: 26781088 5. Feng, W. et al. (2016) Cell discovery 2, 16016. PMID: 27462463 6. Sonneville, R. et al. (2019) eLife 8. PMID: 31545170 7. Wallace, HA. et al. (2014) Development (Cambridge, England) 141, 1332-41. PMID: 24553286 8. Zhang, M. et al. (2012) The Journal of experimental medicine 209, 1703-11. PMID: 22945920 |
| Note | For research use only |
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