Analytical Data
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Gene name
sepA
- Application
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Alternative Names
SEPP1
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Species
Staphylococcus epidermidis
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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
P0C0Q4
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Expression Region
208-507aa
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Molecular Weight
37.7 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
The study of sepA recombinant protein is rooted in the field of molecular biology and its applications in understanding bacterial pathogenesis. SepA, or secreted effector protein A, is a key component secreted by certain pathogens, such as *Pseudomonas aeruginosa*, which is known for its role in mediating virulence and modulating host immune responses. The ability of sepA to influence cellular pathways makes it a significant target for research focused on unraveling the mechanisms of infection and disease. Understanding how sepA functions at the molecular level can provide insights into the interactions between pathogens and host systems, potentially leading to the development of novel therapeutic strategies. The recombination technology allows researchers to produce this protein in a controlled environment, facilitating detailed studies of its structure and function. Furthermore, recombinant sepA can serve as a potential vaccine candidate or a tool for immunological studies, enhancing our understanding of host-pathogen dynamics. Therefore, investigating sepA recombinant protein is crucial for both basic research and applied sciences, contributing to the broader goal of controlling bacterial infections and improving public health outcomes.
