Anti-INPPL1 Antibody Picoband® Fluoro647 Conjugated

SH2-domain containing Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 is an enzyme that in humans is encoded by the INPPL1 gene. The protein encoded by this gene is an SH2-containing 5'-inositol phosphatase that is involved in the regulation of insulin function. The encoded protein also plays a role in the regulation of epidermal growth factor receptor turnover and actin remodelling. Additionally, this gene supports metastatic growth in breast cancer and is a valuable biomarker for breast cancer.

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

Widely expressed, most prominently in skeletal muscle, heart and brain. Present in platelets. Expressed in transformed myeloid cells and in primary macrophages, but not in peripheral blood monocytes.

Actin Assembly, Actin, etc., Angiogenesis, Autoimmune, Cancer, Cardiovascular, Cytoskeleton, Cytoskeleton/ECM, Growth Factors, Immune System Diseases, Immunology, Lipid Signaling, Metabolism, Microfilaments, Neurogenesis, Neurology Process, Neuroscience, Signal Transduction, Signaling Pathway

Phosphatidylinositol (PtdIns) phosphatase that 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. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. 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. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns (3,4,5) P3 thereby regulating membrane ruffling (PubMed:21624956) . Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns (3,4,5) P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma- RIIA receptor (FCGR2A) . Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns (3,4,5) P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF) -induced signaling. May also hydrolyze PtdIns (1,3,4,5) P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification.

1. Habib, T., Hejna, J. A., Moses, R. E., Decker, S. J. Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein. J. Biol. Chem. 273: 18605-18609, 1998. 2. Sleeman, M. W., Wortley, K. E., Lai, K.-M. V., Gowen, L. C., Kintner, J., Kline, W. O., Garcia, K., Stitt, T. N., Yancopoulos, G. D., Wiegand, S. J., Glass, D. J. Absence of the lipid phosphatase SHIP2 confers resistance to dietary obesity. Nature Med. 11: 199-205, 2005. 3. Yu, J., Ryan, D. G., Getsios, S., Oliveira-Fernandes, M., Fatima, A., Lavker, R. M. MicroRNA-184 antagonizes microRNA-205 to maintain SHIP2 levels in epithelia. Proc. Nat. Acad. Sci. 105: 19300-19305, 2008.

Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Membrane; Translocates to membrane ruffles when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. Partly translocated via its SH2 domain which mediates interaction with tyrosine phosphorylated receptors such as the FC-gamma-RIIB receptor (FCGR2B) . Tyrosine phosphorylation may also participate in membrane localization. Insulin specifically stimulates its redistribution from the cytosol to the plasma membrane. Recruited to the membrane following M-CSF stimulation. In activated spreading platelets, localizes with actin at filopodia, lamellipodia and the central actin ring.