Phospho-INPPL1 (Tyr986 + Tyr987) Polyclonal Antibody, PerCP-Cy5.5 Conjugated

The steady state of protein tyrosyl phosphorylation in cells is regulated by the opposing action of tyrosine kinases and protein tyrosine phosphatases (PTPs) . Several groups have independently identified a non transmembrane PTP, designated SHPTP1 (also known as PTP1C, HCP and SHP), which is primarily expressed in hematopoietic cells and characterized by the presence of two SH2 domains N terminal to the PTP domain. A second and much more widely expressed PTP with SH2 domains, SHPTP2 (also designated PTP1D and Syp), has been identified. SHP2 is a protein tyrosine phosphatase that is widely expressed and plays a regulatory role in various cell signaling events that are important for many cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration.

4; 5-trisphosphate 5-phosphatase 2; 51C protein; EC 3.1.3.n1; inositol polyphosphate phosphatase like 1; Inositol polyphosphate phosphatase like protein 1; Inositol polyphosphate phosphatase-like protein 1; INPPL-1; INPPL1; Phosphatidylinositol 3; Phosphatidylinositol 3,4,5 trisphosphate 5 phosphatase 2; Protein 51C; SH2 domain containing inositol 5' phosphatase 2; SH2 domain-containing inositol 5''-phosphatase 2; SH2 domain-containing inositol phosphatase 2; SHIP-2; SHIP2; SHIP2_HUMAN.