产品名称
STT3A Rabbit Polyclonal Antibody
蛋白名称
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A (Oligosaccharyl transferase subunit STT3A) (STT3-A) (EC 2.4.1.119) (B5) (Integral membrane protein 1) (Transmembrane protein TMC)
存储缓冲液
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% New type preservative N.
Human Gene Link
http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&term=3703
Human Swissprot No.
P46977
Human Swissprot Link
https://www.uniprot.org/uniprot/P46977
Mouse Gene Link
http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&term=16430
Mouse Swissprot No.
P46978
Mouse Swissprot Link
https://www.uniprot.org/uniprotkb/P46978/entry
特异性
This antibody detects endogenous levels of STT3A at Human, Mouse
运输及保存条件
-15°C to -25°C/1 year(Do not lower than -25°C)
组织表达
Expressed at high levels in placenta, liver, muscle and pancreas, and at very low levels in brain, lung and kidney. Expressed in skin fibroblasts (at protein level).
细胞定位
Endoplasmic reticulum . Endoplasmic reticulum membrane ; Multi-pass membrane protein .
功能
Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation . N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (By similarity). STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient post-translational glycosylation and mediate glycosylation of sites that have been skipped by STT3A .
