PI 3-kinase C2α Antibody (17): sc-136298

PI 3-kinase C2α Antibody (17) is a mouse monoclonal IgG1 antibody that detects phosphatidylinositol 3-kinase C2α (PI 3-kinase C2α) in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), and immunofluorescence (IF). PI 3-kinase C2α plays a crucial role in cellular signaling pathways by phosphorylating inositol lipids, which are essential for various cellular functions, including cell growth, survival, and metabolism. PI 3-kinase C2α is primarily located in the cytoplasm and is involved in the regulation of membrane trafficking and cytoskeletal dynamics, making anti-PI 3-kinase C2α antibody (17) vital for studying cellular homeostasis and responses to extracellular signals. A C-terminal calcium-binding and phospholipid-binding C2 domain enhances PI 3-kinase C2α′s ability to interact with membranes and other signaling molecules, thereby influencing downstream signaling cascades. PI 3-kinase C2α is expressed in a wide variety of tissues, as indicated by Northern blot analysis revealing an 8 kb mRNA transcript, highlighting PI 3-kinase C2α′s importance in diverse biological processes. With PI 3-kinase C2α′s ability to phosphorylate phosphatidylinositol and phosphatidylinositol-4-phosphate in vitro, PI 3-kinase C2α monoclonal antibody (17) serves as an essential tool for researchers studying lipid metabolism and signaling pathways in various physiological and pathological contexts.

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PI 3-kinase C2α Antibody (17) References:

1. The class II phosphoinositide 3-kinase C2alpha is activated by clathrin and regulates clathrin-mediated membrane trafficking.  |  Gaidarov, I., et al. 2001. Mol Cell. 7: 443-9. PMID: 11239472
2. Phosphoinositide 3-kinase C2alpha is activated upon smooth muscle cell migration and regulated by alpha(v)beta(3) integrin engagement.  |  Paulhe, F., et al. 2002. Biochem Biophys Res Commun. 297: 261-6. PMID: 12237112
3. Individual phosphoinositide 3-kinase C2alpha domain activities independently regulate clathrin function.  |  Gaidarov, I., et al. 2005. J Biol Chem. 280: 40766-72. PMID: 16215232
4. Structural and membrane binding analysis of the Phox homology domain of phosphoinositide 3-kinase-C2alpha.  |  Stahelin, RV., et al. 2006. J Biol Chem. 281: 39396-406. PMID: 17038310
5. Phosphoinositide 3-kinase C2alpha links clathrin to microtubule-dependent movement.  |  Zhao, Y., et al. 2007. J Biol Chem. 282: 1249-56. PMID: 17110375
6. Ca2+-independent, inhibitory effects of cyclic adenosine 5'-monophosphate on Ca2+ regulation of phosphoinositide 3-kinase C2alpha, Rho, and myosin phosphatase in vascular smooth muscle.  |  Azam, MA., et al. 2007. J Pharmacol Exp Ther. 320: 907-16. PMID: 17110524
7. The role of phosphoinositide 3-kinase C2alpha in insulin signaling.  |  Falasca, M., et al. 2007. J Biol Chem. 282: 28226-36. PMID: 17644513
8. Requirement for class II phosphoinositide 3-kinase C2alpha in maintenance of glomerular structure and function.  |  Harris, DP., et al. 2011. Mol Cell Biol. 31: 63-80. PMID: 20974805
9. Phosphoinositide 3-Kinase-C2α Regulates Polycystin-2 Ciliary Entry and Protects against Kidney Cyst Formation.  |  Franco, I., et al. 2016. J Am Soc Nephrol. 27: 1135-44. PMID: 26271513
10. Molecular Basis for Membrane Recruitment by the PX and C2 Domains of Class II Phosphoinositide 3-Kinase-C2α.  |  Chen, KE., et al. 2018. Structure. 26: 1612-1625.e4. PMID: 30293811

The preferred PI 3-kinase C2α antibody is PI 3-kinase C2α Antibody (G-5): sc-365290.