Recombinant Salmonella Typhimurium Virulence Sensor Histidine Kinase Phoq (PHOQ) Protein (his&myc)

Name: Recombinant Salmonella Typhimurium Virulence Sensor Histidine Kinase Phoq (PHOQ) Protein (his&myc)
Brand: Beta LifeScience
SKU: BLC-07022P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Salmonella Typhimurium Virulence Sensor Histidine Kinase Phoq (PHOQ) Protein (his&myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P0DM80
Target Symbol	PHOQ
Species	Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Expression System	E.coli
Tag	N-10His&C-myc
Target Protein Sequence	WWSLRPIEALAREVRELEDHHREMLNPETTRELTSLVRNLNQLLKSERERYNKYRTTLTDLTHSLKTPLAVLQSTLRSLRNEKMSVSKAEPVMLEQISRISQQIGYYLHRASMRGSGVLLSRELHPVAPLLDNLISALNKVYQRKGVNISMDISPEISFVGEQNDFVEVMGNVLDNACKYCLEFVEISARQTDDHLHIFVEDDGPGIPHSKRSLVFDRGQRADTLRPGQGVGLAVAREITEQYAGQIIASDSLLGGARMEVVFGRQHPTQKEE
Expression Range	215-487aa
Protein Length	partial
Mol. Weight	38.5 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance.
Subcellular Location	Cell inner membrane; Multi-pass membrane protein.
Database References	KEGG: stm:STM1230 STRING: 99287.STM1230

Gene Functions References

These data suggest that when Salmonella experiences mildly acidic pH, the virulence regulator PhoP activation requires the sensor protein PhoQ to detect pH and the Salmonella-specific protein UgtL to amplify the PhoQ response. PMID: 28851823
Salmonella enterica Typhimurium, bearing the acidic pH and divalent cation unresponsive phoQ(W104C-A128C) allele is virulent in mice, indicating that acidic pH and divalent cation sensing by PhoQ are dispensable for virulence. PMID: 26002083
Changes in the periplasmic domain of PhoQ lead to conformational movements in the HAMP domain helices which disrupt interaction between the HAMP and the catalytic domains, thus promoting increased kinase activity. PMID: 26015499
study describes a mechanism whereby the transcriptional activator PhoP elicits expression of dissimilar gene sets when its cognate sensor PhoQ is activated by different signals in the periplasm PMID: 24256574
These data demonstrated that Salmonella Typhimurium PhoQ can sense cationic antimicrobial peptides and CRAMP serves as a putative direct PhoPQ activation signal in the mouse intestine. PMID: 22919691
PhoP/Q regulon enables S. Typhimurium to adapt to intramacrophage stresses other than phagolysosomal fusion. PMID: 21511762
RstB-induction increases the levels of phoP mRNA as well as PhoP protein, while lack of the phoPQ genes abolishes RstB-promoted transcription of the PhoP-regulated genes PMID: 20811812
Enzymatic activity of Salmonella typhimurium PhoQ is directly activated by [host] antimicrobial peptides. Our findings reveal a mechanism by which bacteria sense small innate immune molecules to initiate a transcriptional program that promotes virulence PMID: 16096064
induction of PhoP/PhoQ system results in initial surge of PhoP phosphorylation, occupancy of target promoters by PhoP & transcription of PhoP-activated genes; surge by PhoP's positive feedback loop is necessary to jump-start virulence program PMID: 17158330
analysis of signal-dependent regulation in the PhoP/PhoQ system PMID: 18434315
Mutational analysis and NMR spectroscopy of the periplasmic domains of Salmonella typhimurium PhoQ and Pseudomonas aeruginosa PhoQ indicate distinct mechanisms of binding divalent cation. PMID: 18532985
SlyA has a role as a mediator in signal transduction from the PhoP/PhoQ system to other bacterial two-component systems in Salmonella PMID: 18678876
Data report that the PhoP/PhoQ system regulates different Salmonella genes depending on whether the inducing signal is acidic pH or low Mg(2+). PMID: 19801407

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.