

| Catalog No. | HD911012 |
|---|---|
| Description |
Recombinant Human SESN2 Protein, N-His (HD911012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
|
| Expression system | E. coli |
| Accession | P58004 |
| Protein length | Gly66-Thr480 |
| 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 | EC:1.11.1.-, Hi95, Hypoxia-induced gene, SESN2, SEST2, Sestrin-2 |
| Background | Sestrin-2 is a ~54 kDa protein. Functions as an intracellular leucine sensor that negatively regulates the mTORC1 signaling pathway through the GATOR complex. In absence of leucine, binds the GATOR subcomplex GATOR2 and prevents mTORC1 signaling. Binding of leucine to SESN2 disrupts its interaction with GATOR2 thereby activating the TORC1 signaling pathway. This stress-inducible metabolic regulator also plays a role in protection against oxidative and genotoxic stresses. May negatively regulate protein translation in response to endoplasmic reticulum stress, via mTORC1. 1. Budanov, AV. et al. (2008) Cell 134, 451-60. PMID: 18692468 2. Chantranupong, L. et al. (2014) Cell reports 9, 1-8. PMID: 25263562 3. Parmigiani, A. et al. (2014) Cell reports 9, 1281-91. PMID: 25457612 4. Wolfson, RL. et al. (2016) Science (New York, N.Y.) 351, 43-8. PMID: 26449471 5. Saxton, RA. et al. (2016) Science (New York, N.Y.) 351, 53-8. PMID: 26586190 6. Kim, H. et al. (2015) Nature communications 6, 10025. PMID: 26612684 7. Lear, TB. et al. (2019) The Journal of biological chemistry 294, 16527-16534. PMID: 31586034 8. Wang, D. et al. (2022) Molecular cell 82, 770-784.e9. PMID: 35114100 9. Valenstein, ML. et al. (2022) Nature 607, 610-616. PMID: 35831510 10. Jiang, C. et al. (2023) Molecular cell 83, 74-89.e9. PMID: 36528027 |
| Note | For research use only |
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