|Calculated MW||126454 Da|
|Other Names||Phosphatidylinositol 4, 5-bisphosphate 3-kinase catalytic subunit gamma isoform, PI3-kinase subunit gamma, PI3K-gamma, PI3Kgamma, PtdIns-3-kinase subunit gamma, Phosphatidylinositol 4, 5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma, PtdIns-3-kinase subunit p110-gamma, p110gamma, Phosphoinositide-3-kinase catalytic gamma polypeptide, Serine/threonine protein kinase PIK3CG, p120-PI3K, PIK3CG|
|Target/Specificity||A synthetic peptide of in the N-term of human PI3-K p110 gamma was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PI3-kinase (p110) Antibody (subunit gamma) (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Links G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses. Modulates leukocyte chemotaxis to inflammatory sites and in response to chemoattractant agents. May control leukocyte polarization and migration by regulating the spatial accumulation of PIP3 and by regulating the organization of F-actin formation and integrin- based adhesion at the leading edge. Controls motility of dendritic cells. Together with PIK3CD is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in T-lymphocyte migration. Regulates T-lymphocyte proliferation and cytokine production. Together with PIK3CD participates in T-lymphocyte development. Required for B- lymphocyte development and signaling. Together with PIK3CD participates in neutrophil respiratory burst. Together with PIK3CD is involved in neutrophil chemotaxis and extravasation. Together with PIK3CB promotes platelet aggregation and thrombosis. Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of P2Y12 through a lipid kinase activity-independent mechanism. May have also a lipid kinase activity-dependent function in platelet aggregation. Involved in endothelial progenitor cell migration. Negative regulator of cardiac contractility. Modulates cardiac contractility by anchoring protein kinase A (PKA) and PDE3B activation, reducing cAMP levels. Regulates cardiac contractility also by promoting beta-adrenergic receptor internalization by binding to ADRBK1 and by non-muscle tropomyosin phosphorylation. Also has serine/threonine protein kinase activity: both lipid and protein kinase activities are required for beta-adrenergic receptor endocytosis. May also have a scaffolding role in modulating cardiac contractility. Contributes to cardiac hypertrophy under pathological stress. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis.|
|Cellular Location||Cytoplasm. Cell membrane|
|Tissue Location||Pancreas, skeletal muscle, liver and heart.|
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Provided below are standard protocols that you may find useful for product applications.
PI3-Kinases (PI3-Ks) are a family of lipid kinases that are implicated in signal transduction. PI3-K consists of two subunits; p85 and p10. The p85 subunit localize PI3-K activity to the plasma membrane while the p110 subunit contains the catalytic domain of PI3-K (1-2). Four isoforms of p110 has been found; ?, ?, ?, and the ? subunit (3). The gamma isoform is most clostly related to p110 ?, and ? and has been shown not to interact with p85 in vivo (4). It has been found that in p110-gamma protein expression is lost in primary colorectal adeno-carcinomas and in colon cancer cell lines (5)
1. Otsu, M., Hiles, I. D., Gout, I., Fry, M. J., Ruiz-Larrea, F., Panayatou, G., Thompson, A., Dhand, R., Hsuan, J., Totty, N., Smith, A. D., Morgan, S. J., Courtnidge, S. A., Parker, P. J., and Waterfield, M. D. (1992) Cell 65, 91-104
2. Hiles, I. D., Otsu, M., Volinia, S., Fry, M. J., Gout, I., Dhand, R., Panayatou, G., Ruiz-Larrea, F., Thompson, A., Totty, N. F., Hsuan, J. J., Courtnidge, S. A., Parker, P. J., and Waterfield, M. D. (1991) Cell 70, 419-429
3. Hu, P., Mondino, A., Skolnik, E. Y., and Schlessinger, J. (1993) Mol. Cell. Biol. 13, 7677-7688
4. Stoyanov et al. Science 269: 690-693, 1995
5. Sasaki et al. Nature 406: 897-902, 2000.
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