Analytical Data
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Gene name
prsA
- Application
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Alternative Names
prsA; SACOL1897; Foldase protein PrsA; EC 5.2.1.8
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Species
Staphylococcus aureus
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Source
E. coli
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Tag
N- His-SUMO
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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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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 quest to understand the complex processes of protein folding and secretion in bacteria. PrsA, a peptidyl-prolyl isomerase, plays a crucial role in assisting the proper folding of proteins as they are translocated across the bacterial membrane. This protein is particularly significant in gram-positive bacteria, where it is involved in post-translational modifications that are essential for the functionality of secreted proteins. Disruption of prsA can lead to misfolded or inactive proteins, which can negatively affect bacterial growth and virulence. Therefore, understanding prsA's mechanism and its interactions with other cellular components provides valuable insights into microbial physiology and the development of biotechnological applications. Additionally, prsA has garnered attention in the field of protein expression systems, where enhancing its function could improve yields of recombinant proteins in host organisms. Researchers are exploring various expression systems, purification techniques, and folding protocols associated with prsA to optimize the production of therapeutically relevant proteins, making this study not only fundamental for microbiology but also for pharmaceutical biotechnology.
