Analytical Data
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Gene name
OSTa
- Application
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Alternative Names
OSTa；OSTA；Organic solute transporter subunit alpha
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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
Q86UW1
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Expression Region
1-340aa
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AA Sequence
MEPGRTQIKLDPRYTADLLEVLKTNYGIPSACFSQPPTAAQLLRALGPVE LALTSILTLLALGSIAIFLEDAVYLYKNTLCPIKRRTLLWKSSAPTVVSV LCCFGLWIPRSLVLVEMTITSFYAVCFYLLMLVMVEGFGGKEAVLRTLRD TPMMVHTGPCCCCCPCCPRLLLTRKKLQLLMLGPFQYAFLKITLTLVGLF LVPDGIYDPADISEGSTALWINTFLGVSTLLALWTLGIISRQARLHLGEQ NMGAKFALFQVLLILTALQPSIFSVLANGGQIACSPPYSSKTRSQVMNCH LLILETFLMTVLTRMYYRRKDHKVGYETFSSPDLDLNLKA
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Molecular Weight
37.7 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
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Protein Description
OSTa (Oligosaccharyltransferase A) is an essential enzyme involved in the process of glycosylation, a post-translational modification that plays a critical role in protein folding, stability, and function. This enzyme facilitates the transfer of oligosaccharides to asparagine residues in nascent polypeptides, which is crucial for the formation of glycoproteins, a class of proteins that are vital in various biological processes, including cell signaling, immune response, and molecular recognition. The significance of OSTa extends beyond basic cell biology, as aberrations in glycosylation pathways can lead to a range of diseases, including cancer, congenital disorders, and neurodegenerative diseases. Consequently, researchers are focusing on the structural and functional characterization of OSTa to unravel its mechanisms and explore its potential as a therapeutic target. Advances in recombinant protein technology have allowed the production of OSTa in various expression systems, facilitating detailed studies of its enzymatic activity, substrate specificity, and interaction with other cellular components. Understanding the role of OSTa in glycosylation could lead to innovations in drug development and therapies that harness the power of glycoproteins. Furthermore, the study of OSTa and its associated pathways represents a promising area of research with the potential to provide insights into fundamental biological processes and their implications in health and disease.
