Analytical Data
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Gene name
esaB
- Application
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Alternative Names
esaB；Type VII secretion system accessory factor EsaB
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Species
Human
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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
P0C050
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Expression Region
1-80aa
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AA Sequence
MNQHVKVTFDFTNYNYGTYDLAVPAYLPIKNLIALVLDSLDISIFDVNTQIKVMTKGQLLVENDRLIDYQIADGDILKLL
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Molecular Weight
16.6 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
The study of esaB recombinant protein is rooted in the quest to understand bacterial pathogenesis and the immune response it evokes. EsaB, a key component of the Type III secretion system in certain pathogenic bacteria, plays a critical role in injective virulence, allowing these organisms to deliver effector proteins into host cells, thereby manipulating host cellular processes for their survival and proliferation. The manipulation of the esaB gene via recombinant DNA technology enables scientists to produce large quantities of the protein for functional studies. Researchers aim to elucidate the structure-function relationships of esaB, including its role in the secretion mechanism and interaction with host cellular components. Such studies not only advance our understanding of bacterial virulence strategies but also lay the groundwork for the development of novel therapeutic approaches. By investigating the biochemical pathways mediated by esaB, scientists seek to identify potential targets for vaccine development, contributing to the broader effort to combat infections caused by multidrug-resistant pathogens. Overall, the exploration of esaB and its recombinant protein forms is pivotal for advancing molecular microbiology and infectious disease research.
