

| Numéro de catalogue | HD997012 |
|---|---|
| Description |
Recombinant Human TUSC3 Protein, N-His (HD997012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
|
| Système d'expression | E. coli |
| Numéro d'accès | Q13454 |
| Longueur de protéine | Gln42-Pro196 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Espèces | Homo sapiens (Human) |
| Nature | Recombinant |
| Niveau d'endotoxines | Please contact with the lab for this information. |
| Pureté | >90% as determined by SDS-PAGE. |
| Forme | Lyophilized |
| Tampon de stockage | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Reférez-vous aux informations spécifiques sur le tampon dans la copie papier du datasheet ou dans le COA spécifique au lot. |
| 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. |
| Expédition | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Stabilité et stockage | 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. |
| Noms alternatifs | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3, Magnesium uptake/transporter TUSC3, N33, Oligosaccharyl transferase subunit TUSC3, Protein N33, TUSC3, Tumor suppressor candidate 3 |
| Contexte | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3 is a ~39 kDa protein. Acts as accessory component of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Involved in N-glycosylation of STT3B-dependent substrates. Specifically required for the glycosylation of a subset of acceptor sites that are near cysteine residues; in this function seems to act redundantly with MAGT1. In its oxidized form proposed to form transient mixed disulfides with a glycoprotein substrate to facilitate access of STT3B to the unmodified acceptor site. Also has oxidoreductase-independent functions in the STT3B-containing OST complex possibly involving substrate recognition. 1. Zhou, H. et al. (2009) Proceedings of the National Academy of Sciences of the United States of America 106, 15750-5. PMID: 19717468 |
| Note | For research use only |
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