

| Catalog No. | HC172022 |
|---|---|
| Description |
Recombinant Human COMMD1 Protein, N-His (HC172022) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
|
| Expression system | E. coli |
| Accession | Q8N668 |
| Protein length | Ala2-Leu109 |
| 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. |
| 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 | C2orf5, COMM domain-containing protein 1, COMMD1, MURR1, Protein Murr1 |
| Background | COMM domain-containing protein 1 is a ~21 kDa protein. Scaffold protein in the commander complex that is essential for endosomal recycling of transmembrane cargos; the commander complex is composed of the CCC subcomplex and the retriever subcomplex. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL E3 activity and dissociates CAND1 from CUL1 and CUL2. Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Involved in the regulation of membrane expression and ubiquitination of SLC12A2. 1. Healy, MD. et al. (2023) Cell 186, 2219-2237.e29. PMID: 37172566 2. Laulumaa, S. et al. (2024) Nature structural & molecular biology 31, 925-938. PMID: 38459129 3. Mao, X. et al. (2011) The Journal of biological chemistry 286, 32355-65. PMID: 21778237 4. Burstein, E. et al. (2005) The Journal of biological chemistry 280, 22222-32. PMID: 15799966 5. Maine, GN. et al. (2007) The EMBO journal 26, 436-47. PMID: 17183367 6. Thoms, HC. et al. (2010) Cancer research 70, 139-49. PMID: 20048074 7. Smith, L. et al. (2013) American journal of physiology. Cell physiology 305, C133-46. PMID: 23515529 8. Biasio, W. et al. (2004) The Journal of biological chemistry 279, 5429-34. PMID: 14645214 9. Ke, Y. et al. (2010) American journal of physiology. Renal physiology 298, F1445-56. PMID: 20237237 10. Chang, T. et al. (2011) Biochemical and biophysical research communications 411, 506-11. PMID: 21741370 |
| Note | For research use only |
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