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AB236905

Anti-STT3A antibody

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(1 Publication)

Rabbit Polyclonal STT3A antibody. Suitable for IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human STT3A aa 1-150.

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

1 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-STT3A antibody (AB236905)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-STT3A antibody (AB236905)

Paraffin-embedded human pancreatic cancer tissue stained for STT3A using ab236905 at 1/100 dilution in immunohistochemical analysis.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P

applications

Immunogen

Recombinant Fragment Protein within Human STT3A aa 1-150. The exact immunogen used to generate this antibody is proprietary information.

P46977

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "IHCP-species-checked": "testedAndGuaranteed", "IHCP-species-dilution-info": "1/50 - 1/200", "IHCP-species-notes": "<p></p>" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Purification notes
Purity >95%
Storage buffer
pH: 7.4 Preservative: 0.03% Proclin 300 Constituents: PBS, 50% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

STT3A also known as oligosaccharyltransferase 48 kDa subunit plays an important role in the enzymatic process of N-glycosylation specifically as a catalytic subunit in the oligosaccharyltransferase (OST) complex. This protein has a mass of approximately 48 kDa. STT3A is expressed predominantly in rough endoplasmic reticulum membranes where it contributes to the transfer of oligosaccharides onto nascent polypeptide chains a critical step for protein maturation and function.
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.

Defects or dysregulation of STT3A have associations with congenital disorders of glycosylation (CDG) a group of rare inherited metabolic disorders affecting glycoprotein synthesis. Anomalies in STT3A activity can disrupt normal glycoprotein functions leading to a wide range of symptoms including developmental delays and neurological issues. Moreover STT3A dysfunction has connections with cancer progression as altered N-glycosylation patterns are frequently observed in tumor cells affecting proteins such as EGFR and HER2 which are often targets in oncogenesis.
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

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).
See full target information STT3A
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Experimental and therapeutic medicine 24:614 PubMed36160886

2022

TMEM14A aggravates the progression of human ovarian cancer cells by enhancing the activity of glycolysis.

Applications

Unspecified application

Species

Unspecified reactive species

Qingmei Zhang,Xiaohong Wang,Xuan Zhang,Jingfen Zhan,Binbin Zhang,Jin Jia,Jie Chen
View all publications
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