Analytical Data
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Gene name
phoP
- Application
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Alternative Names
phoP；Phosphoethanolamine/phosphocholine phosphatase
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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
P23836
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Expression Region
1-223aa
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AA Sequence
MRVLVVEDNALLRHHLKVQIQDAGHQVDDAEDAKEADYYLNEHIPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRRNSGLASQVISLPPFQVDLSRRELSINDEVIKLTAFEYTIMETLIRNNGKVVSKDSLMLQLYPDAELRESHTIDVLMGRLRKKIQAQYPQEVITTVRGQGYLFELR
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Molecular Weight
29.0 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 regulatory protein involved in the phosphate response signaling pathway in various bacteria, particularly in the model organism Escherichia coli. This protein plays a crucial role in enabling bacteria to adapt to low phosphate conditions by regulating the expression of genes responsible for phosphate acquisition and utilization. The study of PhoP and its recombinant protein form is significant for understanding the mechanisms underlying bacterial adaptation and survival in nutrient-limited environments. Recent research has highlighted PhoP's role not only in phosphate regulation but also in its interactions with other regulatory networks, influencing virulence factors and biofilm formation in pathogens. By utilizing recombinant DNA technology to produce PhoP protein, researchers aim to unravel its structure-function relationships and post-translational modifications. This knowledge can facilitate the development of novel antibacterial strategies, especially considering the rising challenge of antibiotic resistance. Understanding PhoP's regulatory mechanisms can also inspire biotechnological applications, such as optimizing microbial strains for bioremediation or biofertilization. Overall, investigating recombinant PhoP protein offers valuable insights into bacterial physiology and potential applications in health and environmental sustainability.
