ANAPC2 Antibody (H-295): sc-20984

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Comprising more than ten subunits, the anaphase-promoting complex (APC) acts in a cell-cycle dependent manner to promote the separation of sister chromatids during the transition between metaphase and anaphase in mitosis. APC, or cyclosome, accomplishes this progression through the ubiquitination of mitotic cyclins and other regulatory proteins that are targeted for destruction during cell division. APC is phosphorylated, and thus activated, by protein kinases Cdc2/cyclin B and polo-like kinase (Plk). APC is under tight control by a number of regulatory factors, including p55 CDC, E-cadherin and MAD2. Specifically, p55 CDC and E-cadherin directly bind to APC and activate the cyclin-ubiquitination activity of APC. In contrast, MAD2 inhibits APC by forming a ternary complex with p55 CDC and APC and thus preventing APC activation. A heterodimeric complex of either Ubc4 or UbcH10 with ANAPC2 (also known as APC2) and APC11 catalyzes the ubiquitination of human securin and cyclin B1. ANAPC2 contains a C-terminal cullin homology domain that binds both APC11 and UBE2C.