Analytical Data
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Gene name
OPTC
- Application
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Alternative Names
OPTC;OPT;Opticin
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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
Q9UBM4
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Expression Region
20-332aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSASLPRKERKRREEQMPREGDSFEVLPL RNDVLNPDNYGEVIDLSNYEELTDYGDQLPEVKVTSLAPATSISPAKSTT APGTPSSNPTMTRPTTAGLLLSSQPNHGLPTCLVCVCLGSSVYCDDIDLE DIPPLPRRTAYLYARFNRISRIRAEDFKGLTKLKRIDLSNNLISSIDNDA FRLLHALQDLILPENQLEALPVLPSGIEFLDVRLNRLQSSGIQPAAFRAM EKLQFLYLSDNLLDSIPGPLPLSLRSVHLQNNLIETMQRDVFCDPEEHKH TRRQLEDIRLDGNPINLSLFPSAYFCLPRLPIGRFT
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Molecular Weight
38 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
The research on recombinant Oligosaccharide-Probing Transferase Complex (OPTC) has gained significant attention due to its crucial role in glycoprotein biosynthesis and post-translational modifications. OPTC, an essential enzyme complex in glycosylation pathways, is involved in transferring sugar moieties to specific protein substrates, which is vital for their proper functioning and stability. The study of OPTC is particularly important in the context of various diseases, including cancer and genetic disorders, where glycosylation patterns are often disrupted. Recombinant techniques allow for the production of OPTC in controlled laboratory settings, facilitating detailed investigations into its structure, function, and regulatory mechanisms. Advances in genetic engineering and protein expression systems enable researchers to produce large quantities of functional OPTC, making it possible to explore its interactions with other molecules and its role in cellular processes. Understanding the mechanisms governing OPTC activity may lead to novel therapeutic strategies, including the development of engineered glycoproteins with enhanced therapeutic properties. Furthermore, the findings from OPTC research could contribute to the broader field of glycobiology, providing insights into the complexities of glycan-mediated biological interactions and their implications in health and disease.
