Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

Phospho-PAK2 (Ser20) Antibody #2607

Applications Reactivity Sensitivity MW (kDa) Source
W H M GP (R) Endogenous 61 to 67 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  GP=Guinea Pig
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Phospho-PAK2 (Ser20) Antibody detects endogenous levels of PAK2 only when phosphorylated at serine 20. This antibody does not cross-react with other phosphorylated PAK family members.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser20 of human PAK2. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from guinea pig neutrophils stimulated with fMLP for the indicated times, using Phospho-PAK2 (Ser20) Antibody (upper) or PAK1/2/3 Antibody #2604 (lower).

Background

The p21-activated kinase (PAK) family of serine/threonine kinases is engaged in multiple cellular processes, including cytoskeletal reorganization, MAPK signaling, apoptotic signaling, control of phagocyte NADPH oxidase, and growth factor-induced neurite outgrowth (1,2). Several mechanisms that induce PAK activity have been reported. Binding of Rac/Cdc42 to the CRIB (or PBD) domain near the amino terminus of PAK causes autophosphorylation and conformational changes in PAK (1). Phosphorylation of PAK1 at Thr423 by PDK induces activation of PAK1 (3). Several autophosphorylation sites have been identified, including Ser199 and Ser204 of PAK1 and Ser192 and Ser197 of PAK2 (4,5). Because the autophosphorylation sites are located in the amino-terminal inhibitory domain, it has been hypothesized that modification in this region prevents the kinase from reverting to an inactive conformation (6). Research indicates that phosphorylation at Ser144 of PAK1 or Ser139 of PAK3 (located in the kinase inhibitory domain) affects kinase activity (7). Phosphorylation at Ser21 of PAK1 or Ser20 of PAK2 regulates binding with the adaptor protein Nck (8). PAK4, PAK5, and PAK6 have lower sequence similarity with PAK1-3 in the amino-terminal regulatory region (9). Phosphorylation at Ser474 of PAK4, a site analogous to Thr423 of PAK1, may play a pivotal role in regulating the activity and function of PAK4 (10).

  1. Knaus, U.G. and Bokoch, G.M. (1998) Int. J. Biochem. Cell Biol. 30, 857-862.
  2. Daniels, R.H. et al. (1998) EMBO J. 17, 754-764.
  3. King, C.C. et al. (2000) J. Biol. Chem. 275, 41201-41209.
  4. Manser, E. et al. (1997) Mol. Cell. Biol. 17, 1129-1143.
  5. Gatti, A. et al. (1999) J. Biol. Chem. 274, 8022-8028.
  6. Lei, M. et al. (2000) Cell 102, 387-397.
  7. Chong, C. et al. (2001) J. Biol. Chem. 276, 17347-17353.
  8. Zhao, Z. et al. (2000) Mol. Cell. Biol. 20, 3906-3917.
  9. Abo, A. et al. (1998) EMBO J. 17, 6527-6540.
  10. Qu, J. et al. (2001) Mol. Cell. Biol. 21, 3523-3533.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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