Analytical Data
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Gene name
OSTb
- Application
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Alternative Names
OST-B; OSTbeta; OST-beta; Solute carrier family 51 subunit beta
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q80WK2
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Expression Region
Arg54~Ser128
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Molecular Weight
19kDa
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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
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Protein Description
OSTb (Oligosaccharyltransferase beta) is a crucial enzyme involved in the N-glycosylation process, a post-translational modification where sugar moieties are added to proteins. This modification is vital for proper protein folding, stability, and function. Research has indicated that OSTb plays an essential role in various biological processes, including cellular signaling, immune response, and protein quality control. Aberrations in glycosylation processes can lead to multiple diseases, including cancer and genetic disorders. As a result, understanding the structure, function, and mechanisms of OSTb is critical for developing therapeutic strategies targeting glycosylation pathways. Recent advancements in recombinant protein technologies have facilitated the production and study of OSTb in various forms, allowing researchers to manipulate and analyze its function in detail. By exploring the biochemical properties of OSTb and its interactions with substrates, scientists aim to unravel the intricate glycosylation network and its implications in health and disease. This research could also pave the way for novel biopharmaceuticals by harnessing the glycosylation machinery to enhance the efficacy and safety of therapeutic proteins.
