DDOST Protein, Human

DDOST is a key subunit of the oligosaccharyltransferase (OST) complex, which catalyzes the initial glycan transfer during protein N-glycosylation. This co-translational process begins with the transfer of defined glycans to asparagine residues in the nascent polypeptide chain. DDOST Protein, Human is the recombinant human-derived DDOST protein, expressed by E. coli , with tag free. The total length of DDOST Protein, Human is 385 a.a., with molecular weight of ~46 kDa.

DDOST, a subunit of the oligosaccharyl transferase (OST) complex, plays a pivotal role in catalyzing 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. This marks the crucial commencement of protein N-glycosylation, a cotranslational process. The OST complex, where DDOST is a vital component, associates with the Sec61 complex at the translocon complex, facilitating protein translocation across the endoplasmic reticulum (ER). The maximal enzyme activity of the OST complex requires the presence of all subunits. Additionally, DDOST is indispensable for the assembly of both SST3A- and SS3B-containing OST complexes. In essence, DDOST's involvement in protein modification, particularly protein glycosylation, underscores its essential role in initiating the intricate process of N-glycosylation, contributing to the structural and functional diversity of glycoproteins.

Human

E. coli

Tag Free

P39656 (S43-P427)

1650  [NCBI]

Approximately 46 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.