Recombinant Human PHPT1 Protein (His Tag)

Name: Recombinant Human PHPT1 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-3812
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	Q9NRX4
Synonym	CGI-202, HEL-S-132P, HSPC141, PHP14
Background	PHPT1, also known as 14 kDa phosphohistidine phosphatase, phosphohistidine phosphatase 1, protein janus-A homolog, PHP14, is a cytoplasm protein which belongs to thejanus family. PHPT1 / PHP14 is expressed abundantly in heart and skeletal muscle. Phosphatases are a diverse group of enzymes that regulate numerous cellular processes. Much of what is known relates to the tyrosine, threonine, and serine phosphatases, whereas the histidine phosphatases have not been studied as much. Protein histidine phosphorylation exists widely in vertebrates, and it plays important roles in signal transduction and other cellular functions. Protein histidine phosphorylation accounts for about 6% of the total protein phosphorylation in eukaryotic cells. The knowledge about eukaryotic PHPT (protein histidine phosphatase) is still very limited. To date, only one vertebrate PHPT has been discovered, and two crystal structures of human PHPT1 have been solved. PHPT1 / PHP14 can dephosphorylate a variety of proteins (e.g. ATP-citrate lyase and the beta-subunit of G proteins). A putative active site has been identified by its electrostatic character, ion binding, and conserved protein residues.
Description	A DNA sequence encoding the human PHPT1 (Q9NRX4-1) (Ala 2-Tyr 125) was expressed, with a His tag at the N-terminus.
Source	E.coli
Predicted N Terminal	Met
AA Sequence	Ala 2-Tyr 125
Molecular Weight	The recombinant human PHPT1 consisting of 135 a.a. and has a calculated molecular mass of 15.2 kDa as estimated in SDS-PAGE under reducing conditions.
Purity	>97% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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.

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