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Monoclonal Antibody Immunoprecipitation Regulation of Centriole Replication

Also showing Monoclonal Antibody Immunoprecipitation Negative Regulation of Centriole Replication

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: At least five distinct polo-like kinases exist in mammalian cells: PLK1, PLK2, PLK3, PLK4/SAK, and the non-catalytic PLK5 protein (1). The p53-induced PLK2 functions in centriole duplication, as well as at spindle and S phase checkpoints (3-5). Research studies show that PLK2 expression is related to chemosensitivity in ovarian cancer. Downregulation of PLK2 expression in chemosensitive ovarian cancer cells is associated with a greater chance of relapse in patients following specific treatment regimens (6). PLK2 can phosphorylate α-synuclein at Ser129, which is a site shown to be involved in diseases of the central nervous system (7,8). Polo-like kinase 2 also phosphorylates GEFs and GAPs, regulating Ras and Rap small GTPase function in neurons (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The breast cancer susceptibility proteins BRCA1 and BRCA2 are frequently mutated in cases of hereditary breast and ovarian cancers and have roles in multiple processes related to DNA damage, repair, cell cycle progression, transcription, ubiquitination, and apoptosis (1-4). BRCA2 has been shown to be required for localization of Rad51 to sites of double stranded breaks (DSBs) in DNA, and cells lacking BRCA1 and BRCA2 cannot repair DSBs through the Rad51-dependent process of homologous recombination (HR) (5). Numerous DNA damage-induced phosphorylation sites on BRCA1 have been identified, including Ser988, 1189, 1387, 1423, 1457, 1524, and 1542, and kinases activated in a cell cycle-dependent manner, including Aurora A and CDK2, can also phosphorylate BRCA1 at Ser308 and Ser1497, respectively (6-10). Cell cycle-dependent phosphorylation of BRCA2 at Ser3291 by CDKs has been proposed as a mechanism to switch off HR as cells progress beyond S-phase by blocking the carboxy terminal Rad51 binding site (11).