Anti-phospho-SHIP2, (Tyr497) (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2, SH2 Domain-

SHIP2, also known as 'phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2,' is a cytoplasmic protein that translocates to membrane ruffles when activated, due to different stimulus and cell type. It belongs to the inositol-1,4,5-trisphosphate 5-phosphatase family with a SAM (sterile alpha motif) domain and a SH2 domain. SHIP2 specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways and also in regulating PI3K-dependent insulin signaling, EGF signaling pathway and a signaling pathway that regulates actin cytoskeleton remodeling. SHIP2 is required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. It regulates cell adhesion, cell spreading and neuritogenesis and acts as a negative regulator of EPHA2 receptor endocytosis and of the FC-gamma-RIIA receptor (FCGR2A). SHIP2 mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Expression is widely seen in most tissues but primarily in skeletal muscle, heart, brain and transformed myeloid cells and in primary macrophages, but not in peripheral blood monocytes. Applications: Suitable for use in Western Blot and Immunohistochemistry. Other applications not tested. Recommended Dilution: Western Blot: 0.01-0.1ug/ml, Immunohistochemistry (formalin fixed paraffin embedded): 5ug/ml, Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.