SHP1 (Tyr-536), Phosphospecific Antibody

SHP1 (PTP1C, SH-PTP1, or HCP) is a protein-tyrosine phosphatase (PTP) involved in cell migration, cell proliferation, and immune cell function. This phosphatase contains two N-terminal SH2 domains and a C-terminal phosphatase domain. SHP1 associates with a variety of cytokine and growth factor receptors and regulates signal transduction through dephosphorylation of these receptors or their downstream effectors. Downstream of receptor activation, SHP1 regulates the transcriptional activity stimulated by JAK/Stat and MAPK pathways. SHP1 activity is regulated by both tyrosine and serine phosphorylation. Phosphorylation of Tyr-536 and Tyr-564 stimulates phosphatase activity and promotes interaction with Grb-2. Serine phosphorylation at Ser-591 is mediated by PKCα and leads to inhibition of phosphatase activity. Thus, phosphorylation at tyrosine relative to serine residues may be regulated by different cell signaling pathways to control SHP1 activity.

Phospho-SHP1 (Tyr-536) synthetic peptide (coupled to carrier protein) corresponding to amino acids around tyrosine 536 in human SHP1. The sequence is highly conserved in rat and mouse SHP1.

This antibody was cross-adsorbed to a non-specific phospho-tyrosine peptide then affinity-purified using phospho-SHP1 (Tyr-536) peptide. The antibody detects a 68 kDa* band on SDS-PAGE immunoblots of human Jurkat cells treated with pervanadate, but is not observed in control cells.