Analytical Data
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Gene name
epiA
- Application
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Alternative Names
epiA；PUM；Mucin-1
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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
P08136
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Expression Region
31-52aa
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AA Sequence
IASKFICTPGCAKTGSFNSYCC
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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
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Protein Description
EpiA is a protein that has garnered attention in the field of molecular biology and biotechnology due to its potential applications in therapeutic interventions and biocatalysis. It is associated with various biological processes, including bacterial virulence and immune response modulation. The ability to produce recombinant EpiA enables researchers to study its structure and function in detail, which can provide insights into its role in pathogenesis and its interactions with host systems. Furthermore, the recombinant production of EpiA allows for the development of engineered variants that may enhance its functional properties or alter its interactions with other biomolecules. This research is particularly significant in the context of understanding infectious diseases, where targeting specific protein interactions may lead to novel treatment strategies. Additionally, the study of EpiA may contribute to the broader understanding of protein folding and stability, which are critical for designing effective biomolecules for biotechnological applications. The ongoing exploration of EpiA through recombinant techniques highlights its potential as a valuable tool in both basic and applied research, paving the way for innovations in drug development and protein engineering.
