Recombinant Human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B (STT3B), partial

Code CSB-YP823456HU
MSDS
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Source Yeast
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Code CSB-EP823456HU
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Source E.coli
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Code CSB-EP823456HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP823456HU
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Source Baculovirus
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Code CSB-MP823456HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
STT3B
Uniprot No.
Alternative Names
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B; Homolog of yeast STT3; Oligosaccharyl transferase subunit STT3B; SIMP; source of immunodominant MHC associated peptides; Source of immunodominant MHC-associated peptides homolog; STT3 subunit of the oligosaccharyltransferase complex homolog B (S. cerevisiae); STT3 subunit of the oligosaccharyltransferase complex homolog B; STT3-B; Stt3b; STT3B_HUMAN
Species
Homo sapiens (Human)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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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
  1. Study reports that STT3B-oligosaccharyltransferase, but not STT3A-oligosaccharyltransferase, is a lipid-linked oligosaccharide hydrolase. PMID: 30181269
  2. These results reveal that the oxidoreductase activity of the STT3B-containing oligosaccharyltransferase is necessary for dengue virus infection. PMID: 28720733
  3. 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
  4. 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
  5. Results show homozygous mutation in STT3A and in STT3B causes congenital disorders of glycosylation. PMID: 23842455
  6. Extreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST. PMID: 23530066
  7. Data show that prolonged transthyretin (TTR) unfolding induces externalization of cryptic N-glycosylation site and triggers STT3B-dependent posttranslational N-glycosylation. PMID: 22607976
  8. 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
  9. 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

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Involvement in disease
Congenital disorder of glycosylation 1X (CDG1X)
Subcellular Location
Endoplasmic reticulum. Endoplasmic reticulum membrane; Multi-pass membrane protein.
Protein Families
STT3 family
Tissue Specificity
Expressed in heart, brain, placenta, lung, liver, muscle, kidney and pancreas. Expressed in skin fibroblasts (at protein level).
Database Links

HGNC: 30611

OMIM: 608605

KEGG: hsa:201595

STRING: 9606.ENSP00000295770

UniGene: Hs.475812

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