Name :
Recombinant Human PHPT1 Protein (His Tag), HPLC-verified
Biological Activity :
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.
Biological Activity :
Testing in progress
Expression Host :
Human
Source :
E. coli
Tag :
Protein Accession No. :
Q9NRX4-1
NCBI Gene ID :
Synonyms :
Synonyms :
phosphohistidine Phosphatase 1
Amino Acid Sequence :
Molecular Weight :
The recombinant human PHPT1 consisting of 135 amino acids 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. ≥ 95 % as determined by SEC-HPLC.
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
Please contact us for more information.
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.
Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
CGI-202 Protein, Human; HEL-S-132P Protein, Human; HSPC141 Protein, Human; PHP14 Protein, Human PHPT1 背景信息 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.
References & Citations :
Busam,R.D. et al., 2006, J Biol Chem. 281 (45):33830-4. Zhang,X.Q. et al., 2009, Ups J Med Sci.114 (2):65-72. Gong,W. et al., 2009, Biochem J. 418 (2):337-44. Chapin,L.J. et al., 2009, J Exp Bot. 60 (7):2179-90.
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