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AB116946

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

1 Images
SDS-PAGE - Recombinant Human STT3A protein (AB116946)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human STT3A protein (AB116946)

12.5% SDS-PAGE showing ab116946 at approximately 36.52kDa stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

Tag free

Applications

SDS-PAGE, WB, ELISA

applications

Biologically active

No

Accession

P46977

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.3% Glutathione

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>Recombinant protein.</p>" } } }

Sequence info

[{"sequence":"GGSTDTGKHIKENDYYTPTGEFRVDREGSPVLLNCLMYKMCYYRFGQVYTEAKRPPGFDRVRNAEIGNKDFELDVLEEAYTTEHWLVRIYKVKDLDNRG","proteinLength":"Fragment","predictedMolecularWeight":"36.52 kDa","actualMolecularWeight":null,"aminoAcidEnd":701,"aminoAcidStart":603,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"P46977","tags":[]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

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.

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.

Product protocols

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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