

| Catalog No. | HC225012 |
|---|---|
| Description |
Recombinant Human EMC2 Protein, N-His (HC225012) expressed in E. coli, spanning Met1-Ser297. Purity: >90% by SDS-PAGE.
Highlights
|
| Expression system | E. coli |
| Accession | Q15006 |
| Protein length | Met1-Ser297 |
| 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 | 37.00 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 | EMC2, ER membrane protein complex subunit 2, KIAA0103, TPR repeat protein 35, TTC35, Tetratricopeptide repeat protein 35 |
| Background | ER membrane protein complex subunit 2 is a ~34 kDa protein. Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. 1. Guna, A. et al. (2018) Science (New York, N.Y.) 359, 470-473. PMID: 29242231 2. Shurtleff, MJ. et al. (2018) eLife 7. PMID: 29809151 3. Chitwood, PJ. et al. (2018) Cell 175, 1507-1519.e16. PMID: 30415835 4. Pleiner, T. et al. (2020) Science (New York, N.Y.) 369, 433-436. PMID: 32439656 5. O'Donnell, JP. et al. (2020) eLife 9. PMID: 32459176 6. Pleiner, T. et al. (2021) Molecular cell 81, 2693-2704.e12. PMID: 33964204 |
| Note | For research use only |
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