Analytical Data
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Gene name
ipaC
- Application
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Alternative Names
ipaC；ipaC；Type 3 secretion system translocon Protein SctB
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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
P18012
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Expression Region
1-363aa
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AA Sequence
MEIQNTKPTQTLYTDISTKQTQSSSETQKSQNYQQIAAHIPLNVGKNPVLTTTLNDDQLLKLSEQVQHDSEIIARLTDKKMKDLSEMSHTLTPENTLDISSLSSNAVSLIISVAVLLSALRTAETKLGSQLSLIAFDATKSAAENIVRQGLAALSSSITGAVTQVGITGIGAKKTHSGISDQKGALRKNLATAQSLEKELAGSKLGLNKQIDTNITSPQTNSSTKFLGKNKLAPDNISLSTEHKTSLSSPDISLQDKIDTQRRTYELNTLSAQQKQNIGRATMETSAVAGNISTSGGRYASALEEEEQLISQASSKQAEEASQVSKEASQATNQLIQKLLNIIDSINQSKNSAASQIAGNIRA
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Molecular Weight
38.7 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 ipaC protein, a significant virulence factor derived from the bacterium Shigella flexneri, plays a crucial role in the pathogenesis of shigellosis, a severe form of bacterial dysentery. This protein is central to the bacterium's ability to invade and manipulate host cells, facilitating its entry into epithelial tissues and evading the immune response. Research on ipaC has garnered attention due to its potential as a target for therapeutic intervention and vaccine development. Understanding its structure and function can provide insights into the molecular mechanisms underpinning Shigella's pathogenicity. Moreover, the study of ipaC’s interactions with host cell signaling pathways is essential for elucidating how Shigella orchestrates its invasion strategy. Recent advances in recombinant protein technology have enabled the production of ipaC in host systems, allowing for detailed biochemical characterization and the investigation of its immunogenic properties. As a result, ipaC holds promise not only for developing novel vaccination strategies but also for designing inhibitors that could disrupt its function, thereby mitigating the impact of shigellosis. The continuous exploration of ipaC's biological roles, combined with innovative approaches in molecular biology, is pivotal for advancing our understanding of bacterial pathogenesis and developing effective countermeasures against this significant public health challenge.
