Recombinant Human PHPT1/PHP14 Protein (His Tag) | PKSH030832

Recombinant Human PHPT1/PHP14 Protein (His Tag) | PKSH030832 | Gentaur US, UK & Europe Disrtribition

Synonyms: CGI-202;HEL-S-132P;HSPC141;PHP14

Active Protein: N/A

Activity: A DNA sequence encoding the human PHPT1 (Q9NRX4-1) (Ala 2-Tyr 125) was expressed, with a polyhistidine tag at the N-terminus.

Protein Construction: A DNA sequence encoding the human PHPT1 (Q9NRX4-1) (Ala 2-Tyr 125) was expressed, with a polyhistidine tag at the N-terminus.

Fusion Tag: N-His

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 97 % as determined by reducing SDS-PAGE.

Endotoxin: Please contact us for more information.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 15.2 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

Reconstitution: Please refer to the printed manual for detailed information.

Background: PHPT1, also known as 14 kDa phosphohistidine phosphatase, phosphohistidine phosphatase 1, protein janus-A homolog, PHP14, is a cytoplasm protein which belongs to the janus 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.

Research Area: N/A