epitope mapping within an internal region of PSK2 of human origin
recommended for detection of PSK2 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
PSK2 Background Information The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions in eukaryotes, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the serine/threonine (Ser/Thr) protein kinases. PSK2 (Prostate-derived STE20-like kinase 2), also known as TAOK1 (TAO kinase 1), TAO1 (thousand and one amino acid protein 1), hKFC-B (kinase from chicken homolog B), MARKK or MAP3K16, is a member of the Ser/Thr protein kinase family and belongs to the GCK-like class of STE20-like kinases. Expressed at high levels in testis and at lower levels in placenta, colon, brain and skeletal muscle, PSK2 localizes to the cytoplasm and phosphorylates MEK-3, thereby activating the p38 MAP kinase pathway. In addition, PSK2 is capable of activating JNK and inducing JNK-dependent morphological changes that lead to apoptosis. Upon activation of caspases, PSK2 is cleaved by caspase-3.
