Purified anti-PLK-1

PLK-1 (polo-like kinase 1) is a member of te serine/threonine protein kinase family, cdc5/polo subfamily. Highly homologous to polo-like kinase (Drosophila), PLK-1 contains two polo box domains with a predicted molecular weight of 68 kD. This nuclear protein is highly expressed in placenta and colon and has been shown to regulate cdc2/cyclin B through phosphorylation and activation of cdc25c phosphatase. PLK-1 may also be required for cell division; depletion of PLK-1 results in apoptosis. PLK-1 is upregulated by growth stimulating agents and is regulated by cell cycle position (highest in G2/M phase, declining to nearly undetectable levels after mitosis and throughout G1). PLK-1 is modified by phosphorylation (Thr210 is the major phosphorylation site in activated PLK-1 from mitotic cells) and has been shown to interact with nuclear distribution gene C. The 3F8 monoclonal antibody recognizes human and mouse PLK-1 and has been shown to be useful for Western blotting.