PHPT1 Human, Active
PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Description
PHPT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (1-125a.a.) and having a molecular mass of 15.9kDa.
PHPT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
PHPT1, a member of the Janus protein family, is a 125-amino acid protein. This protein exists as a monomer in the cytoplasm and functions as an EDTA-insensitive phosphohistidine phosphatase. When overexpressed, PHPT1 exhibits specific phosphatase activity towards phosphopeptide I, without any activity towards phosphotyrosine, phosphothreonine, or phosphoserine peptides.
Produced in E. coli, PHPT1 is a single, non-glycosylated polypeptide chain consisting of 145 amino acids (1-125a.a.) and possesses a molecular mass of 15.9 kDa. This protein includes a 20 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
The PHPT1 protein solution (concentration: 0.5mg/ml) is formulated in a buffer consisting of 20mM Tris-HCl (pH 8.0), 0.2M NaCl, 2mM DTT, and 10% glycerol.
The specific activity of the enzyme is measured as greater than 120 units/mg. This is defined as the quantity of enzyme required to hydrolyze 1 nanomole of p-nitrophenyl phosphate per minute at a pH of 7.5 and a temperature of 37°C.
PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.
MGSSHHHHHH SSGLVPRGSH MAVADLALIP DVDIDSDGVF KYVLIRVHSA PRSGAPAAES KEIVRGYKWA EYHADIYDKV SGDMQKQGCD CECLGGGRIS HQSQDKKIHV YGYSMAYGPA QHAISTEKIK AKYPDYEVTW ANDGY.
Product Science Overview
PHPT1 catalyzes the reversible dephosphorylation of histidine residues in proteins. This activity is essential for the regulation of various cellular functions, including the dephosphorylation of G-beta and ATP citrate lyase . Additionally, PHPT1 negatively regulates CD4 T lymphocytes by dephosphorylating and inhibiting KCa3.1 channels .
Interestingly, PHPT1 has been shown to dephosphorylate not only phosphohistidine but also phospholysine residues in chemically phosphorylated histone H1 and polylysine . This broader substrate specificity highlights the enzyme’s versatility and potential involvement in diverse cellular processes.
