Recombinant Human STT3A protein
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Recombinant Human STT3A protein is a Human Fragment protein, in the 603 to 701 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
ITM1, TMC, STT3A, Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A, Oligosaccharyl transferase subunit STT3A, STT3-A, B5, Integral membrane protein 1, Transmembrane protein TMC
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human STT3A protein (AB116946)
12.5% SDS-PAGE showing ab116946 at approximately 36.52kDa stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
STT3A is part of the OST complex which catalyzes the transfer of glycan from a lipid donor to asparagine residues on nascent polypeptides in a process known as co-translational N-glycosylation. This modification is essential for proper protein folding stability and activity. The OST complex with STT3A as a catalytic core is fundamental in eukaryotic cells affecting the function of numerous glycoproteins. It interacts with various components within the endoplasmic reticulum to ensure efficient glycosylation.
Pathways
The involvement of STT3A extends to the protein processing in endoplasmic reticulum pathway and is integral to the broader process of protein folding and quality control. This pathway ensures proper protein configuration and prevents the accumulation of misfolded proteins. STT3A functionally relates to proteins like calnexin and calreticulin which work in the calnexin/calreticulin cycle to assist in the folding of glycoproteins indicating its important role in maintaining protein homeostasis in cells.
Specifications
Form
Liquid
General info
Function
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 (PubMed : 31831667, PubMed : 34653363). 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 (PubMed : 19167329).
Sequence similarities
Belongs to the STT3 family.
Target data
Product promise
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