Phospho-PAK (T402) Antibody Summary
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Detection of Phospho-PAK (T402) by Western Blot. Western blot of rat hippocampal lysate showing specific immunolabeling of the approximately 68-70 kDa PAK protein (Control). The phosphospecificity of this labeling is shown in the second lane ( lambda-phosphatase: lambda PPase). The blot is identical to the control except that it was incubated in lambda PPase (1200 units for 30 minutes) before being exposed to the anti-Phospho-PAK-1, 2, 3 (T402). The immunolabeling of PAK is completely eliminated by treatment with lambda PPase.
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PAK (p21-activated kinase) is a general term for a Serine/Threonine kinase that functions downstream of Rho-family GTPases to regulate cytoskeletal (actin) structure and gene transcription. There are two mammalian PAK groups, each with three members. Group I contains PAK-1/ alpha -PAK, PAK-2/ beta -PAK and PAK-3/ gamma -PAK; group II contains PAKs 4-6. All PAKs contain p21-binding domains and a kinase domain. Only group I PAKs are activated by Cdc42 (cell division cycle 24) and exist as dimers. The dimeric form of group I PAKs keep them in an inactive state. This is due to cross-inhibition from one monomer to another. Following p21 binding, these PAKs dissociate and undergo either auto-, or exogenous (PKD1) phosphorylation on a kinase domain Threonine that is embedded in an 18 aa sequence that is absolutely conserved in PAKs 1-3 in both rat and human. In rat, this Threonine occurs at 402 in PAK-2, T422 in PAK-1, and T421 in PAK-3. In human, each position is increased by one (i.e. T403 vs. T402 in rat PAK-2, etc.). Phosphorylation at this homologous site activates the PAKs, which, following additional regulatory phosphorylations, can then interact with desmin, myosin light chain kinase, LIM1, filamin A and/or Merlin. Preparation Prepared from rabbit serum by affinity purification via sequential chromatography
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