Human Recombinant DDOST protein (V2LY-0526-LY3518)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Protein Construction
This product is Human Recombinant DDOST protein consist of Amino Acid: 43-427 and predicts a molecular mass of 42.7 kDa.
Molecule Mass
42.7 kDa
Sequence
Amino Acid: 43-427
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
≥90% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
dolichyl-diphosphooligosaccharide-protein glycosyltransferase
Function
Essential 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. Required for the assembly of both SST3A- and SS3B-containing OST complexes. Required for efficient N-glycosylation.

Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc3Man9GlcNAc2 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 (By similarity).

Required for the assembly of both SST3A- and SS3B-containing OST complexes (PubMed:22467853).
Biological Process
Neutrophil degranulation Source: Reactome
Protein glycosylation Source: UniProtKB
Protein N-linked glycosylation Source: UniProtKB
Protein N-linked glycosylation via asparagine Source: GO_Central
Regulation of protein stability Source: ARUK-UCL
Response to cytokine Source: UniProtKB
T cell activation Source: UniProtKB
Viral protein processing Source: Reactome
Cellular Location
Endoplasmic reticulum membrane
Involvement in disease
Congenital disorder of glycosylation 1R (CDG1R):
A form of congenital disorder of glycosylation, a multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
Topology
Lumenal: 43-427
Helical: 428-447
Cytoplasmic: 448-456
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For research use only. Not intended for any clinical use.

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