Analytical Data
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Gene name
DDOST
- Application
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Alternative Names
DDOST；KIAA0115；OST48；Dolichyl-diphosphooligosaccharide--Protein glycosyltransferase 48 kDa subunit
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P39656
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Expression Region
1-456aa
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AA Sequence
MGYFRCAGAGSFGRRRKMEPSTAARAWALFWLLLPLLGAVCASGPRTLVL LDNLNVRETHSLFFRSLKDRGFELTFKTADDPSLSLIKYGEFLYDNLIIF SPSVEDFGGNINVETISAFIDGGGSVLVAASSDIGDPLRELGSECGIEFD EEKTAVIDHHNYDISDLGQHTLIVADTENLLKAPTIVGKSSLNPILFRGV GMVADPDNPLVLDILTGSSTSYSFFPDKPITQYPHAVGKNTLLIAGLQAR NNARVIFSGSLDFFSDSFFNSAVQKAAPGSQRYSQTGNYELAVALSRWVF KEEGVLRVGPVSHHRVGETAPPNAYTVTDLVEYSIVIQQLSNGKWVPFDG DDIQLEFVRIDPFVRTFLKKKGGKYSVQFKLPDVYGVFQFKVDYNRLGYT HLYSSTQVSVRPLQHTQYERFIPSAYPYYASAFSMMLGLFIFSIVFLHMK EKEKSD
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Molecular Weight
77 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
DDOST, or Dolichyl-Diphosphooligosaccharide-Protein Glycosyltransferase, is an essential enzyme that plays a pivotal role in the N-glycosylation process, which is critical for protein folding and function in eukaryotic cells. Emerging as a significant focus in biochemical research, DDOST catalyzes the transfer of pre-assembled oligosaccharides onto nascent polypeptides within the endoplasmic reticulum, facilitating proper protein maturation and stability. Disturbances in DDOST function have been associated with various diseases, including genetic disorders and cancers, underscoring its importance in cellular homeostasis. The study of DDOST’s role in glycosylation is crucial for understanding how glycomic changes affect physiological and pathological processes. Furthermore, the potential therapeutic applications of manipulating DDOST activity or its pathways to treat related diseases highlight the importance of ongoing research in this area. By creating recombinant forms of DDOST, scientists aim to elucidate its structural and functional properties, leading to innovations in targeted therapies and biotechnological applications. The investigation of DDOST also promises to provide insights into glycosylation patterns that could serve as biomarkers for disease diagnosis and treatment stratification. As such, the exploration of DDOST as a protein model forms a critical dimension in the fields of glycobiology, biochemistry, and pharmaceutical science, paving the way for advances in understanding complex biological systems and developing novel therapeutic strategies.
