{"product_id":"cst-5472t","title":"CST,  5472T, Phospho-PLK1 (Thr210) Antibody","description":"Polyclonal Antibody for studying PLK1 (Thr210) phosphate. Validated for Western Blotting. Available in 2 sizes. Highly specific and rigorously validated in-house, Phospho-PLK1 (Thr210) Antibody (CST #5472) is ready to ship.\n\n\u003cb\u003eProduct Usage Information\u003c\/b\u003e\nWestern Blotting: 1:1000\n\u003cb\u003eStorage\u003c\/b\u003e\nSupplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg\/ml BSA and 50% glycerol. Store at -20°C. Do not aliquot the antibody.\n\u003cb\u003eProtocol\u003c\/b\u003e\nAvailable protocols: Western Blotting\n\u003cb\u003eSpecificity \/ Sensitivity\u003c\/b\u003e\nPhospho-PLK1 (Thr210) Antibody detects endogenous levels PLK1 only when phosphorylated at threonine 210.\nSpecies Reactivity: Human\n\u003cb\u003eSource \/ Purification\u003c\/b\u003e\nPolyclonal antibodies are produced by immunizing animals with a synthetic phospho-peptide corresponding to residues surrounding Thr210 of human PLK1. Antibodies are purified using protein A and peptide affinity chromatography.\n\u003cb\u003eBackground\u003c\/b\u003e\nAt least four distinct polo-like kinases exist in mammalian cells: PLK1, PLK2, PLK3, and PLK4\/SAK (1). PLK1 apparently plays many roles during mitosis, particularly in regulating mitotic entry and exit. The mitosis promoting factor (MPF), cdc2\/cyclin B1, is activated by dephosphorylation of cdc2 (Thr14\/Tyr15) by cdc25C. PLK1 phosphorylates cdc25C at Ser198 and cyclin B1 at Ser133, causing translocation of these proteins from the cytoplasm to the nucleus (2-5). PLK1 phosphorylation of Myt1 at Ser426 and Thr495 has been proposed to inactivate Myt1, one of the kinases known to phosphorylate cdc2 at Thr14\/Tyr15 (6). Polo-like kinases also phosphorylate the cohesin subunit SCC1, causing cohesin displacement from chromosome arms that allow for proper cohesin localization to centromeres (7). Mitotic exit requires activation of the anaphase promoting complex (APC) (8), a ubiquitin ligase responsible for removal of cohesin at centromeres, and degradation of securin, cyclin A, cyclin B1, Aurora A, and cdc20 (9). PLK1 phosphorylation of the APC subunits Apc1, cdc16, and cdc27 has been demonstrated and has been proposed as a mechanism by which mitotic exit is regulated (10,11). Substitution of Thr210 with Asp has been reported to elevate PLK1 kinase activity and delay\/arrest cells in mitosis, while a Ser137Asp substitution leads to S-phase arrest (12). In addition, while DNA damage has been found to inhibit PLK1 kinase activity, the Thr210Asp mutant is resistant to this inhibition (13). PLK1 has been reported to be phosphorylated at Ser137 and Thr210 in mitosis; DNA damage prevents phosphorylation at these sites (14).\n\u003cb\u003eAlternate Names\u003c\/b\u003e\ncell cycle regulated protein kinase; PLK; PLK-1; PLK1; polo (Drosophia)-like kinase; polo like kinase; polo like kinase 1; Polo-like kinase 1; polo-like kinase 1 (Drosophila); Serine\/threonine-protein kinase 13; Serine\/threonine-protein kinase PLK1; STPK13\n\n\u003cb\u003eSpecification\u003c\/b\u003e\n\nREACTIVITY: H\nSENSITIVITY: Endogenous\nMW (kDa): 62\nSOURCE: Rabbit","brand":"CST","offers":[{"title":"Default Title","offer_id":46799812329641,"sku":"5472T","price":0.99,"currency_code":"USD","in_stock":true}],"url":"https:\/\/iright.com\/products\/cst-5472t","provider":"Iright","version":"1.0","type":"link"}