Analytical Data
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Gene name
PhoP
- Application
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Alternative Names
phoP; b1130; JW1116; Transcriptional regulatory protein PhoP
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Species
Escherichia coli
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Source
HEK293
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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
P23836
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Expression Region
1-223aa
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Molecular Weight
29.5 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
PhoP is a key transcriptional regulator in various bacterial species, particularly in the context of pathogenicity and virulence. It belongs to the two-component signal transduction systems, which are crucial for bacteria to sense and respond to environmental changes. In many pathogenic strains, such as *Salmonella* and *Mycobacterium tuberculosis*, PhoP plays a significant role in regulating genes associated with their survival and adaptation within host environments. Understanding the function and mechanisms of PhoP is essential for deciphering bacterial pathogenesis and could potentially lead to new therapeutic strategies. Researchers often focus on producing recombinant PhoP protein to study its structure, functional domains, and interactions with DNA and other proteins. Techniques such as recombinant DNA technology enable the expression and purification of PhoP, facilitating insights into its regulatory roles and involvement in stress responses. Investigating PhoP can also provide information on its potential as a target for antibiotic development, particularly in the face of increasing antibiotic resistance. Overall, the study of PhoP and its recombinant protein forms is crucial for a deeper understanding of bacterial physiology and the development of novel antimicrobial therapies.
