Analytical Data
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Gene name
OSTb
- Application
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Alternative Names
OSTb;OSTB;Organic solute transporter subunit beta
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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
Q86UW2
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Expression Region
1-128aa
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AA Sequence
MEHSEGAPGDPAGTVVPQELLEEMLWFFRVEDASPWNHSILALAAVVVIISMVLLGRSIQASRKEKMQPPEKETPEVLHLDEAKDHNSLNNLRETLLSEKPNLAQVELELKERDVLSVFLPDVPETES
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Molecular Weight
14.3 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
OSTb (Oligosaccharyltransferase beta) is a crucial enzyme involved in the process of N-glycosylation, a post-translational modification essential for the proper folding, stability, and function of glycoproteins. In recent years, the study of OSTb has gained significant attention due to its role in various biological processes and its implications in diseases such as cancer and congenital disorders. The enzymatic activity of OSTb is pivotal in transferring oligosaccharides to nascent polypeptides as they emerge from the ribosome, ensuring that glycoproteins acquire their necessary glycans. These modifications are critical for cell-cell communication, immune response, and protein stability. As a result, understanding the structural and functional properties of OSTb can provide insights into its mechanisms of action, as well as its potential as a therapeutic target. The recombinant production of OSTb has facilitated detailed studies on its enzymatic activity, substrate specificity, and interaction with other cellular components. Recent advances in biotechnology have enabled the generation of high-yield OSTb protein, allowing for in-depth investigations into its biological functions and its role in various cellular pathways. Such research not only enhances our fundamental understanding of glycosylation but also opens avenues for the development of novel therapeutic strategies aimed at manipulating glycosylation pathways in diseases where OSTb activity is altered. Overall, OSTb and its associated research represent a promising frontier in both basic and applied biological sciences, highlighting the complexity of glycoprotein synthesis and its far-reaching implications in health and disease.











