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STT3A Antibody (Center)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | P46977 |
| Other Accession | Q2KJI2, P46978, Q5RCE2 |
| Reactivity | Human |
| Predicted | Bovine, Mouse |
| Host | Rabbit |
| Clonality | polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 80530 Da |
| Gene ID | 3703 |
|---|---|
| Other Names | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A, Oligosaccharyl transferase subunit STT3A, STT3-A, 2.4.99.18, B5, Integral membrane protein 1, Transmembrane protein TMC, STT3A, ITM1, TMC |
| Target/Specificity | This STT3A antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 476-507 amino acids from the Central region of human STT3A. |
| Dilution | WB~~1:2000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | STT3A Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | STT3A (HGNC:6172) |
|---|---|
| Synonyms | ITM1, TMC |
| 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). |
| Cellular Location | Endoplasmic reticulum. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P46978}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P46978} |
| Tissue Location | 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) |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Catalytic subunit 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. 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). SST3A seems to be involved in complex substrate specificity. 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 cotranslational glycosylation and mediate glycosylation of sites that have been skipped by STT3A.
References
Hong G.,et al.Genomics 31:295-300(1996).
Lissy N.A.,et al.Biochim. Biophys. Acta 1306:137-141(1996).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Kalnine N.,et al.Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
Taylor T.D.,et al.Nature 440:497-500(2006).
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