

| Catalog No. | MD364012 |
|---|---|
| Description |
Recombinant Mouse TRIM72 Protein, N-His (MD364012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
|
| Expression system | E. coli |
| Accession | Q1XH17 |
| Protein length | Ala287-Ala477 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Mus musculus (Mouse) |
| 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 | EC:2.3.2.27, Mg53, Mitsugumin-53, Trim72, Tripartite motif-containing protein 72 |
| Background | Tripartite motif-containing protein 72 is a ~52 kDa protein. Muscle-specific E3 ubiquitin-protein ligase that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Its ubiquitination activity is mediated by E2 ubiquitin-conjugating enzymes UBE2D1, UBE2D2 and UBE2D3. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. 1. Cai, C. et al. (2009) Nature cell biology 11, 56-64. PMID: 19043407 2. Park, SH. et al. (2023) Nature structural & molecular biology 30, 1695-1706. PMID: 37770719 3. Masumiya, H. et al. (2009) Channels (Austin, Tex.) 3, 6-11. PMID: 19202355 4. Cai, C. et al. (2009) The Journal of biological chemistry 284, 3314-3322. PMID: 19029292 |
| Note | For research use only |
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