Analytical Data
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Gene name
prsA
- Application
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Alternative Names
prsA；TBP1；26S proteasome regulatory subunit 6A
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Species
E.coli
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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
Q5HET4
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Expression Region
21-320aa
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AA Sequence
CGASATDSKENTLISSKAGDVTVADTMKKIGKDQIANASFTEMLNKILADKYKNKVNDKKIDEQIEKMQKQYGGKDKFEKALQQQGLTADKYKENLRTAAYHKELLSDKIKISDSEIKEDSKKASHILIKVKSKKSDKEGLDDKEAKQKAEEIQKEVSKDPSKFGEIAKKESMDTGSAKKDGELGYVLKGQTDKDFEKALFKLKDGEVSEVVKSSFGYHIIKADKPTDFNSEKQSLKEKLVDQKVQKNPKLLTDAYKDLLKEYDVDFKDRDIKSVVEDKILNPEKLKQGGAQGGQSGMSQ
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Molecular Weight
49.6 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 study of prsA recombinant protein is rooted in the understanding of protein folding and secretion pathways in bacteria, particularly in *Bacillus subtilis*, where prsA plays a crucial role. PrsA (Protein Disulfide Isomerase A) functions as a chaperone that assists in the correct folding of secretory proteins, ensuring they achieve their functional conformations and are properly exported outside the cell. Misfolded proteins can lead to cellular stress and reduced efficiency in protein secretion, which is vital for various biotechnological applications. The prsA gene has garnered attention for its potential to improve the yield and activity of recombinant proteins expressed in prokaryotic systems. Recent studies have highlighted its significance in enhancing the secretion and stability of therapeutic proteins, enzymes, and industrially relevant biomolecules. By optimizing prsA expression and functionality, researchers aim to enhance the efficiency of protein production processes, addressing challenges associated with protein misfolding and aggregation. Consequently, prsA serves as a pivotal target in the ongoing efforts to streamline bioproduction systems, making it a focal point for research and industrial application in recombinant protein technology.
