Analytical Data
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Gene name
epiA
- Application
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Alternative Names
epiALantibiotic epidermin
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Species
Staphylococcus epidermidis
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Source
E. coli
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Tag
N- His-KSI
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08136
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Expression Region
31-52aa
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Molecular Weight
17.7 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
Related Products
Protein Description
EpiA, a protein with potential implications in various biological processes, has garnered attention in the fields of microbiology and cellular biology. It is primarily associated with the regulation of bacterial pathogenesis and biofilm formation. The study of EpiA recombination is driven by its potential role in understanding how bacteria adapt to environmental changes and develop resistance to antibiotics. Recent research highlights EpiA's involvement in the modulation of gene expression related to virulence factors, suggesting its significance in bacterial survival and pathogenicity. By employing techniques such as gene cloning, site-directed mutagenesis, and recombinant protein expression systems, scientists aim to elucidate the structure-function relationship of EpiA. This research not only hopes to clarify the molecular mechanisms governing bacterial behavior but also seeks to pave the way for novel therapeutic targets in combating bacterial infections. Additionally, the ability of EpiA to influence biofilm dynamics presents opportunities for developing strategies to disrupt biofilm-associated infections, which are notoriously difficult to treat. Thus, the investigation of EpiA recombinants is a crucial step towards understanding bacterial adaptability and improving infection control methodologies.
