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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-PAK1 (Ser199/204)/PAK2 (Ser192/197) Antibody #2605

Filter:
  • WB
Western Blotting Image 1: Phospho-PAK1 (Ser199/204)/PAK2 (Ser192/197) Antibody
Western blot analysis of extracts from guinea pig neutrophils stimulated with fMLP (1 µM ) for the indicated times, using Phospho-PAK1 (Ser199/204)/PAK2 (Ser192/197) Antibody.

To Purchase # 2605

Cat. # Size Qty. Price Ships
2605T 20 µl
$146
2605S 100 µl
$357

Supporting Data

REACTIVITY H M R GP
SENSITIVITY Endogenous
MW (kDa) 61 to 67 (PAK2), 68 to 74 (PAK1/3)
SOURCE Rabbit
Application Key:
  • WB-Western Blotting 
Species Cross-Reactivity Key:
  • H-Human 
  • M-Mouse 
  • R-Rat 
  • GP-Guinea Pig 
  • Related Products

Product Information

Product Usage Information

Application Dilution
Western Blotting 1:1000

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

Phospho-PAK1 (Ser199/204)/PAK2 (Ser192/197) Antibody detects endogenous levels of Ser199/204 phosphorylated PAK1 or Ser192/197 phosphorylated PAK2. It may also detect Ser200/205 phosphorylated PAK3, however it does not cross-react with phosphorylated PAK4.

Species Reactivity:

Human, Mouse, Rat, Guinea Pig

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding serine 199/204 of human PAK1. Antibodies are purified by protein A and peptide affinity chromatography.

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, PAK5/7, 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). PAK family members are widely expressed, and often overexpressed in human cancer (11,12).

Pathways

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