Analytical Data
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Gene name
FkpA
- Application
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Alternative Names
Rotamase yzzS
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P45523
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Expression Region
26-270aa
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Molecular Weight
33.2 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
FkpA (folding helper protein A) is a key protein involved in the proper folding of other proteins, particularly in the periplasmic space of Gram-negative bacteria. It belongs to the peptidyl-prolyl cis-trans isomerase (PPIase) family, which facilitates the folding process by catalyzing the isomerization of proline residues in polypeptides. Understanding the role of FkpA in protein folding is crucial, as misfolded proteins can lead to various diseases and cellular dysfunctions. Its function also has significant implications in biotechnology and pharmaceuticals, where recombinant proteins are often produced in bacterial systems. Research has increasingly focused on the characterization of FkpA's structure and its interaction with target substrates. This involves investigating its enzymatic properties and the mechanisms by which it enhances the solubility and activity of proteins, especially those that are prone to aggregation. Furthermore, studies have shown that FkpA can be an essential component for the efficient production of therapeutic proteins, making it a target of interest for engineering more effective microbial expression systems. Continued exploration of FkpA may provide insights into new strategies for improving protein yield and functionality in industrial applications and offer potential therapeutic avenues in treating diseases linked to protein misfolding.
