Analytical Data
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Gene name
eaeA
- Application
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Alternative Names
Attaching and effacing protein Outer membrane protein
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Species
Hafnia alvei
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P52869
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Expression Region
1-280aa
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Molecular Weight
46.1 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 eaeA, a gene encoding the enteropathogenic Escherichia coli (EPEC) adhesion factor, has garnered significant interest in the field of microbiology and infectious disease research. EPEC is a leading cause of diarrheal disease, particularly in infants and young children in developing countries. The eaeA gene plays a critical role in the adherence of EPEC to intestinal epithelial cells, facilitating the formation of characteristic attaching and effacing lesions that disrupt normal intestinal function. Researchers have focused on understanding the molecular mechanisms underlying eaeA expression and its regulation, as well as the role of the Eae protein in host-pathogen interactions. Recombined forms of the eaeA protein are being investigated for their potential use in vaccine development and therapeutics aimed at preventing EPEC infections. By exploring the structural and functional characteristics of the eaeA protein, scientists aim to identify key epitopes that could elicit a robust immune response and provide protection against this pathogen. Overall, the exploration of eaeA recombinant proteins represents a promising avenue for advancing our understanding of EPEC pathogenesis and developing effective strategies to combat this significant public health challenge.
