Recombinant Human 14 Kda Phosphohistidine Phosphatase (PHPT1) Protein (His)

Name: Recombinant Human 14 Kda Phosphohistidine Phosphatase (PHPT1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-04185P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human 14 Kda Phosphohistidine Phosphatase (PHPT1) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9NRX4
Target Symbol	PHPT1
Synonyms	14 kDa phosphohistidine phosphatase; CGI 202; HSPC141; Phosphohistidine phosphatase 1; PHP14; PHP14_HUMAN; PHPT1; Protein janus A homolog; Protein janus-A homolog; Sex regulated protein janus a
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	MAVADLALIPDVDIDSDGVFKYVLIRVHSAPRSGAPAAESKEIVRGYKWAEYHADIYDKVSGDMQKQGCDCECLGGGRISHQSQDKKIHVYGYSMAYGPAQHAISTEKIKAKYPDYEVTWANDGY
Expression Range	1-125aa
Protein Length	Full Length
Mol. Weight	15.8kDa
Research Area	Cell Biology
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	Exhibits phosphohistidine phosphatase activity.
Subcellular Location	Cytoplasm.
Protein Families	Janus family
Database References	HGNC: 30033 OMIM: 610167 KEGG: hsa:29085 STRING: 9606.ENSP00000247665 UniGene: Hs.409834
Tissue Specificity	Expressed abundantly in heart and skeletal muscle.

Gene Functions References

In the process of assay optimization, we discovered that PHPT1 is sensitive to a reducing environment and inhibited by transition-metal ions, with one apparent Cu(II) binding site with IC50 value of 500 +/- 20 muM and two apparent Zn(II) binding sites with IC50 values of 25 +/- 1 and 490 +/- 20 muM PMID: 29630837
High PHPT1 expression is associated with cancer. PMID: 29787434
H2O2 exposure induces selective oxidation of hPHPT1 at Met95, a residue within the substrate binding region. Molecular dynamics simulations suggest that if Met95 oxidation alters hPHPT1 activity, then it will do so by altering the stability of an intermediate state. Mass spectrometry showed that H2O2-induced oxidation does not impact hPHPT1 function negatively. PMID: 27034094
PHPT1 was expressed in the epithelium of proximal tubuli and nuclei of clear-cell renal cell carcinoma tissue samples. PMID: 26537769
PHPT1 can dephosphorylate phospholysine in chemically phosphorylated histone H1 and polylysine PMID: 25574816
The specific degradation of the PHPT1 splice variant indicates that the quality control and the self-guarding of the cellular system works at two levels, first at the RNA level and proteasome level. PMID: 25450458
the histidine phosphatase, protein histidine phosphatase 1, inhibits NDPK-B-activated TRPV5 in inside/out patch experiments. PMID: 24523290
Overexpression of PHP by the use of a plasmid vector, pIRES2-AcGFP1-PHP, induced apoptosis in HUVEC PMID: 21967643
Significantly higher expression levels of PHPT1 protein were found in lung cancer samples than in normal tissues adjacent to lung cancer. PMID: 21163124
these data implicate regulatory roles for PHPT1 in a G protein-sensitive step involved in nutrient-induced insulin secretion PMID: 20501872
These results demonstrate for the first time that PHP14 may be functionally important in lung cancer cell migration and the invasion of lung cancer cells, mediated partly through modulation of actin cytoskeleton rearrangement. PMID: 19344975
Northern blot analysis indicated that the human phosphohistidine phosphatase mRNA was present preferentially in heart and skeletal muscle. PMID: 12383260
In the present work, we have searched for potential active site residues in the human phosphohistidine phosphatase by point mutations of conserved histidine and arginine residues to alanine. PMID: 16219293
Overexpression of PHP results in increased dephosphorylation with concomitant inactivation of ACL, thus finally leading to cell damage. PMID: 18656514
PHPT-1 functions to negatively regulate CD4 T cells PMID: 18796614
Solution structure and catalytic mechanism of human protein histidine phosphatase 1. PMID: 18991813
results suggest that an increased activity of protein histidine phosphatase (PHP) impairs neuron cellular function whereas downregulation of PHP does not PMID: 19138678

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.