PAK6 (N-terminal region) Antibody

P21-activated kinase 6 (PAK6) is a member of the PAK family of serine/threonine kinases. These kinases have a highly conserved amino-terminal Cdc42/Rac interactive binding domain and a carboxyl-terminal kinase domain. PAK kinases are implicated in the regulation of a number of cellular processes, including cytoskeleton rearrangement, apoptosis and the MAP kinase signaling pathway. PAK6 interacts with the androgen receptor, a steroid hormone transcription factor involved in male sexual differentiation and development. PAK6 is highly expressed in testis and prostate tissues. Regulation of PAK6 kinase activity occurs through multiple sites of phosphorylation. Activation of PAK6 requires autophosphorylation of Ser-560 and MKK-6 induced phosphorylation of Tyr-566. In addition, p38 MAPK can phosphorylate Ser-165, which increases PAK6 kinase activity. Thus, multiple signaling pathways may regulate the activity of PAK6 through differential phosphorylation.

A synthetic peptide (coupled to carrier protein) corresponding to amino acids in the N-terminal region of human PAK6. The sequence used has two amino acid differences compared to rat and mouse PAK6.

The antibody detects a 75 kDa* band on SDS-PAGE immunoblots of human PAK6 recombinant protein. This reactivity is specifically blocked by pre-incubation with PAK6 (N-terminal) peptide and is not affected by lambda phosphatase treatment.