Product Details

Full Product Name

Rabbit anti-Homo sapiens (Human) STT3B Polyclonal antibody

Uniprot No.

Q8TCJ2

Target Names

STT3B

Alternative Names

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B antibody; Homolog of yeast STT3 antibody; Oligosaccharyl transferase subunit STT3B antibody; SIMP antibody; source of immunodominant MHC associated peptides antibody; Source of immunodominant MHC-associated peptides homolog antibody; STT3 subunit of the oligosaccharyltransferase complex homolog B (S. cerevisiae) antibody; STT3 subunit of the oligosaccharyltransferase complex homolog B antibody; STT3-B antibody; Stt3b antibody; STT3B_HUMAN antibody

Raised in

Rabbit

Species Reactivity

Human

Immunogen

Recombinant Human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B protein (682-809AA)

Immunogen Species

Homo sapiens (Human)

Conjugate

HRP

Clonality

Polyclonal

Isotype

IgG

Purification Method

>95%, Protein G purified

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4

Form

Liquid

Tested Applications

ELISA

Protocols

ELISA Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Target Background

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. 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. STT3B is present in a small subset of OST complexes and mediates both cotranslational and post-translational N-glycosylation of target proteins: STT3B-containing complexes are required for efficient post-translational glycosylation and while they are less competent than STT3A-containing complexes for cotranslational glycosylation, they have the ability to mediate glycosylation of some nascent sites that are not accessible for STT3A. STT3B-containing complexes also act post-translationally and mediate modification of skipped glycosylation sites in unfolded proteins. Plays a role in ER-associated degradation (ERAD) pathway that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins by mediating N-glycosylation of unfolded proteins, which are then recognized by the ERAD pathway and targeted for degradation. Mediates glycosylation of the disease variant AMYL-TTR 'Asp-38' of TTR at 'Asn-118', leading to its degradation.

Gene References into Functions

Study reports that STT3B-oligosaccharyltransferase, but not STT3A-oligosaccharyltransferase, is a lipid-linked oligosaccharide hydrolase. PMID: 30181269
These results reveal that the oxidoreductase activity of the STT3B-containing oligosaccharyltransferase is necessary for dengue virus infection. PMID: 28720733
STT3B was significantly upregulated in hip osteoarthritis with affected versus intact cartilage, particularly in the analysis of hypertrophic and normotrophic compared with atrophic bone remodelling pattern. PMID: 27974301
Post-translational modification of cotranslationally skipped sites by STT3B is hindered by the middle X residue, resulting in hypoglycosylation of consensus sites containing large hydrophobic and negatively charged side chains. PMID: 25029371
Results show homozygous mutation in STT3A and in STT3B causes congenital disorders of glycosylation. PMID: 23842455
Extreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST. PMID: 23530066
Data show that prolonged transthyretin (TTR) unfolding induces externalization of cryptic N-glycosylation site and triggers STT3B-dependent posttranslational N-glycosylation. PMID: 22607976
The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein. PMID: 19167329
STT3 proteins are the catalytic subunits of the oligosaccharyltransferase. Vertebrate, plant and insect genomes have an STT3A gene and a STT3B gene. SIMP is a member of the STT3B subfamily of STT3 proteins. PMID: 12887896