Analytical Data
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Gene name
phoQ
- Application
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Alternative Names
(Sensor histidine protein kinase/phosphatase PhoQ)
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Species
Salmonella typhimurium
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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
P0DM80
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Expression Region
215-487aa
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Molecular Weight
38.5 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
PhoQ protein, a key component of the PhoPQ two-component regulatory system, plays a crucial role in the virulence and adaptation of various bacterial pathogens. This system enables bacteria, such as Salmonella and Escherichia coli, to sense environmental signals and modulate their responses accordingly, particularly under stress conditions like low magnesium or acidic environments. The PhoQ protein acts as a sensor kinase, phosphorylating itself upon detection of specific stimuli and subsequently activating the response regulator PhoP, which then regulates gene expression related to virulence factors, antimicrobial resistance, and biofilm formation. Understanding the structure and function of PhoQ is essential for elucidating its role in bacterial pathogenicity and resistance mechanisms. The recombinant expression of PhoQ allows for in-depth biochemical studies, including protein-protein interactions and structural analyses, which are vital for the development of targeted therapeutics. By manipulating this protein, researchers aim to disrupt its signaling pathways, potentially leading to new strategies to combat bacterial infections and enhance the efficacy of existing antibiotics. Given the rising concern over antibiotic resistance, the study of PhoQ and its interactions with other cellular components remains a significant area of investigation within microbiology and infectious disease research.
