Analytical Data
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Gene name
hlyE
- Application
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Alternative Names
hlyE；clyA；hpr；sheA；Hemolysin E. chromosomal
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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
P77335
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Expression Region
2-182aa
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AA Sequence
TEIVADKTVEVVKNAIETADGALDLYNKYLDQVIPWQTFDETIKELSRFKQEYSQAASVLVGDIKTLLMDSQDKYFEATQTVYEWCGVATQLLAAYILLFDEYNEKKASAQKDILIKVLDDGITKLNEAQKSLLVSSQSFNNASGKLLALDSQLTNDFSEKSSYFQSQVDKIRKEAYAGAA
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Molecular Weight
21.2 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 hlyE gene, coding for the Hemolysin E protein, has garnered significant attention in microbial pathogenesis and protein engineering research. Originally identified in various pathogenic strains of bacteria, particularly in the context of enterohemorrhagic Escherichia coli (EHEC), hlyE plays a pivotal role in bacterial virulence by contributing to cell lysis and facilitating tissue invasion. Its ability to induce cytolytic effects makes it a focal point for studies aimed at understanding bacterial-host interactions. Researchers are investigating the mechanisms by which hlyE disrupts cellular membranes, aiming to elucidate its structure-function relationships. Additionally, as a candidate for vaccine development and therapeutic applications, recombinant hlyE protein is being explored for its potential to enhance immune responses. The production of recombinant hlyE in various expression systems allows for detailed structural and functional characterizations, paving the way for novel antimicrobial strategies. Furthermore, understanding this protein's role in pathogenesis could lead to innovations in diagnosing and treating infections caused by hemolytic bacteria. Thus, hlyE serves as a crucial model for studying microbial virulence factors and advancing biotechnological applications in medicine and vaccine development.
