Analytical Data
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Gene name
ipaC
- Application
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Alternative Names
42 kDa antigen
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Species
Shigella flexneri
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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
P18012
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Expression Region
1-363aa
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Molecular Weight
46.2 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
Related Products
Protein Description
The study of ipaC recombinant protein is rooted in the field of microbiology and immunology, particularly in the context of understanding the pathogenic mechanisms of enteropathogenic bacteria such as Shigella flexneri. IpaC is a key effector protein secreted by the type III secretion system (T3SS), playing a critical role in bacterial invasion and manipulation of host cell signaling pathways. Research into ipaC has garnered interest due to its potential as a target for vaccine development and therapeutic interventions against shigellosis, a significant public health concern in many developing countries. Characterization of ipaC's structure and function is essential for elucidating its role in the bacterial lifecycle and host-pathogen interactions. Studies utilizing recombinant technology have enabled the production of ipaC in sufficient quantities for functional assays and immunogenicity testing, thereby advancing our understanding of its biochemical properties and potential applications in vaccines. By exploring the immunological responses elicited by ipaC in animal models, researchers aim to establish its efficacy as a candidate for protective vaccines, which could significantly reduce the incidence of infections caused by Shigella spp. and similar pathogens. Overall, ongoing research into ipaC recombinant protein not only enhances our comprehension of bacterial pathogenesis but also contributes to the development of innovative strategies to combat infectious diseases.
