Analytical Data
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Gene name
prgI
- Application
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Alternative Names
prgI；prgI；SPI-1 type 3 secretion system needle filament Protein
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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
P41784
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Expression Region
1-80aa
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AA Sequence
MATPWSGYLDDVSAKFDTGVDNLQTQVTEALDKLAAKPSDPALLAAYQSKLSEYNLYRNAQSNTVKVFKDIDAAIIQNFR
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Molecular Weight
56.6 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
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Protein Description
The study of PrgI recombinant protein has garnered significant interest due to its potential role in the field of microbial biology and its implications for understanding bacterial pathogenesis. PrgI is a component of type III secretion systems (T3SS) found in various pathogenic bacteria, including enteropathogenic Escherichia coli and Salmonella. These systems are crucial for the translocation of effector proteins into host cells, facilitating bacterial invasion and immune evasion. Investigating PrgI can provide insights into the molecular mechanisms underlying these processes. Moreover, understanding the structural and functional characteristics of PrgI could pave the way for the development of novel therapeutic strategies aimed at disrupting T3SS function, thereby increasing the efficacy of treatments against bacterial infections. The recombinant expression of PrgI allows for detailed studies of its properties and interactions, enabling researchers to elucidate its role within the T3SS and assess its potential as a target for vaccine development. With the rising concern of antibiotic resistance, innovative approaches like targeting T3SS components highlight the importance of such studies in the pursuit of new antimicrobial strategies.
