MilliporeSigma™ Phosphohistidine (pHis) , Rabbit, Unlabeled, Polyclonal,

Description

• Phosphorylation plays an important role in regulating protein activities and various cellular signaling events in cells
• Limited by the tools available for phosphohistidine (pHis) detection, the majority of studies focus on serine, threonine, and tyrosine phosphorylations
• Histidine phosphorylation can occur at either N1 (1-pHis) or N3 (3-pHis) of the imidazole ring
• The development of stable phosphoryltriazolylalanine analogues of pHis (pTza and pPza) allows the generation of antibodies for studying both histidine N1 and N3 phosphorylations in signaling events
• There is growing evidence implicating His kinases in cancer and tumor metastasis and the first metastasis suppressor gene identified is one of the two known mammalian His kinases, Nm23-H1 (also known as NME1, nucleoside diphosphate kinase, or NDPK-A)
• Nm23-H1/NME1 and the closely related Nm23-H2 (NME2/NDPK-B) catalyze the transfer of phosphate from ATP onto Nucleoside-diphosphates (NDPs) through a 1-pHis enzyme intermediate
• Nm23-H1/-H2 also possess His kinase activity, transferring the phosphate from the active site pHis onto a His in a target protein
• Metabolic enzymes such as phosphoglycerate mutase (PGAM), succinyl CoA synthase (SCS), and ATP citrate lyase (ACL) also use pHis as an enzyme intermediate
• Unlike NME1/2, PGAM uses 3-pHis as an enzyme intermediate
• In addition to eukaryotes, histidine phosphorylation is well documented in bacterial two-component signaling pathways involved in chemotaxis, although the phosphate is transferred from the pHis formed in the receptor/sensor protein to Asp residues of an acceptor response regulator protein, and the receptor/sensor protein essentially functions as an aspartate kinase.