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Human TUSC3 Recombinant Protein (N-His) (HD997012)

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Overview
Catalog No.HD997012
Description
Recombinant Human TUSC3 Protein, N-His (HD997012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% as determined by SDS-PAGE.
Expression systemE. coli
AccessionQ13454
Protein lengthGln42-Pro196
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesHomo 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 NamesDolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3, Magnesium uptake/transporter TUSC3, N33, Oligosaccharyl transferase subunit TUSC3, Protein N33, TUSC3, Tumor suppressor candidate 3
Background

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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Formula
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Formula
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