Phospho-PBK/TOPK (Thr9) Antibody detects endogenous levels of PBK/TOPK only when phosphorylated at threonine 9.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to amino acids around Thr9 of human PBK/TOPK. Antibodies are purified by protein A and affinity chromatography.
Background
PBK/TOPK is a serine/threonine kinase that is phosphorylated and active during mitosis (1). PBK/TOPK is composed of kinase subdomains and a carboxy-terminal PDZ-Binding domain, which is thought to interact with the tumor suppressor protein hDlg (1). Increased PBK/TOPK expression has been observed in highly proliferative malignant cell lines, and PBK/TOPK expression is strongly downregulated during terminal differentiation of HL-60 leukemic cells (2,3). PMA-induced kinase activity toward PBK/TOPK has been observed (4), and cdc2/cyclinB has been shown to phosphorylate PBK/TOPK in vitro, presumably at Thr9 (1). Potential substrates of PBK/TOPK include p38 MAPK and c-Myc (3,4).