|Calculated MW||122762 Da|
|Other Names||Phosphatidylinositol 4, 5-bisphosphate 3-kinase catalytic subunit beta isoform, PI3-kinase subunit beta, PI3K-beta, PI3Kbeta, PtdIns-3-kinase subunit beta, Phosphatidylinositol 4, 5-bisphosphate 3-kinase 110 kDa catalytic subunit beta, PtdIns-3-kinase subunit p110-beta, p110beta, PIK3CB, PIK3C1|
|Target/Specificity||A synthetic peptide of human PI3-K p110 beta 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 beta) (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4- phosphate) and 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. Involved in the activation of AKT1 upon stimulation by G-protein coupled receptors (GPCRs) ligands such as CXCL12, sphingosine 1-phosphate, and lysophosphatidic acid. May also act downstream receptor tyrosine kinases. Required in different signaling pathways for stable platelet adhesion and aggregation. Plays a role in platelet activation signaling triggered by GPCRs, alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) and ITAM (immunoreceptor tyrosine-based activation motif)-bearing receptors such as GP6. Regulates the strength of adhesion of ITGA2B/ ITGB3 activated receptors necessary for the cellular transmission of contractile forces. Required for platelet aggregation induced by F2 (thrombin) and thromboxane A2 (TXA2). Has a role in cell survival. May have a role in cell migration. Involved in the early stage of autophagosome formation. Modulates the intracellular level of PtdIns3P (Phosphatidylinositol 3-phosphate) and activates PIK3C3 kinase activity. May act as a scaffold, independently of its lipid kinase activity to positively regulate autophagy. May have a role in insulin signaling as scaffolding protein in which the lipid kinase activity is not required. May have a kinase-independent function in regulating cell proliferation and in clathrin-mediated endocytosis. Mediator of oncogenic signal in cell lines lacking PTEN. The lipid kinase activity is necessary for its role in oncogenic transformation. Required for the growth of ERBB2 and RAS driven tumors.|
|Cellular Location||Cytoplasm. Nucleus. Note=Interaction with PIK3R2 is required for nuclear localization and export|
|Tissue Location||Expressed ubiquitously.|
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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 beta isoform forms heterodimers with p85 subunit (4). p110-beta has a role in regulating the formation and stability of integrin adhesion bonds (alpha-2B and beta-3), which are necessary for shear force-induced platelet activation (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. Jackson et al. Nature Med. 11: 507-514, 2005.
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