Recombinant Human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit(DDOST)

Code CSB-CF006594HU
Product Type Transmembrane Protein
Size Pls inquiry other sizes
Uniprot No. P39656
Storage Buffer Lyophilized from Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Species Homo sapiens (Human)
Sequence SGPRTLVLLDNLNVRETHSLFFRSLKDRGFELTFKTADDPSLSLIKYGEFLYDNLIIFSPSVEDFGGNINVETISAFIDGGGSVLVAASSDIGDPLRELGSECGIEFDEEKTAVIDHHNYDISDLGQHTLIVADTENLLKAPTIVGKSSLNPILFRGVGMVADPDNPLVLDILTGSSTSYSFFPDKPITQYPHAVGKNTLLIAGLQARNNARVIFSGSLDFFSDSFFNSAVQKAAPGSQRYSQTGNYELAVALSRWVFKEEGVLRVGPVSHHRVGETAPPNAYTVTDLVEYSIVIQQLSNGKWVPFDGDDIQLEFVRIDPFVRTFLKKKGGKYSVQFKLPDVYGVFQFKVDYNRLGYTHLYSSTQVSVRPLQHTQYERFIPSAYPYYASAFSMMLGLFIFSIVFLHMKEKEKSD
Source in vitro E.coli expression system
Gene Names DDOST
Protein Names Recommended name: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit Short name= DDOST 48 kDa subunit Short name= Oligosaccharyl transferase 48 kDa subunit EC= 2.4.1.119
Expression Region 43-456
Tag Info N-terminal 10xHis-tagged
Protein Description Full Length of Mature Protein
Storage Store at -20°C, for extended storage, conserve at -20°C or -80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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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.
Involvement in disease Congenital disorder of glycosylation 1R (CDG1R)
Subcellular Location Endoplasmic reticulum membrane, Single-pass type I membrane protein
Protein Families DDOST 48 kDa subunit family
Database Links

HGNC: 2728

OMIM: 602202

KEGG: hsa:1650

STRING: 9606.ENSP00000364188

UniGene: Hs.523145

Pathway Protein processing in endoplasmic reticulum

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