Analytical Data
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Gene name
esaA
- Application
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Species
Staphylococcus aureus
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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
P0C049
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Expression Region
483-821aa
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Molecular Weight
46.0 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 EsaA recombinant protein revolves around its potential role in understanding bacterial pathogenesis, particularly in the context of infectious diseases. EsaA is a protein associated with the type III secretion system (T3SS), a critical virulence mechanism employed by many pathogenic bacteria, especially those within the genera like *Pseudomonas* or *Salmonella*. This system allows bacteria to inject effector proteins directly into host cells, facilitating infection and evading immune responses. Research into EsaA focuses on elucidating its structure, functional characteristics, and interactions with host cells, as it may serve as a key component in the pathogenicity of T3SS-dependent bacteria. Moreover, studying the recombinant form of EsaA provides insights into its immunogenic properties, which could pave the way for developing novel vaccines or therapeutic interventions. Understanding how EsaA and similar proteins operate offers significant implications for designing strategies to combat bacterial infections, enhancing our knowledge of microbial resistance and host-pathogen interactions.
