Analytical Data
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Gene name
PrgJ
- Application
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Alternative Names
PrgJ；Birc1b；Naip-rs6；Baculoviral IAP repeat-containing Protein 1b
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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
P41785
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Expression Region
1-101aa
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AA Sequence
MSIATIVPENAVIGQAVNIRSMETDIVSLDDRLLQAFSGSAIATAVDKQTITNRIEDPNLVTDPKELAISQEMISDYNLYVSMVSTLTRKGVGAVETLLRS
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Molecular Weight
12.2 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
PrgJ, a key component in the pathogenicity of various bacteria, particularly in the context of type III secretion systems (T3SS), has garnered significant attention in microbiological research. T3SSs are sophisticated molecular injectors that enable bacteria to translocate effector proteins into host cells, facilitating infection. PrgJ, as a membrane protein, plays a critical role in the assembly and regulation of this secretion system, affecting the virulence and survival of bacteria such as Salmonella typhimurium and Yersinia pestis. Understanding the structure and function of PrgJ is essential for dissecting the mechanisms by which these pathogens hijack host cellular processes. Recent advancements in recombinant protein techniques have enabled researchers to produce and purify PrgJ for in-depth biochemical studies, including structural characterization and interaction assays. This research not only aims to elucidate the molecular functions of PrgJ within the T3SS but also has potential implications for developing therapeutic strategies against bacterial infections. By targeting components like PrgJ, novel antimicrobial therapies could be designed to inhibit the T3SS, ultimately reducing the virulence of pathogenic bacteria and enhancing treatment options for infectious diseases.
