p21-activated kinases (PAKs) bind activated Cdc42 and Rac via a Cdc42/Rac interactive binding (CRIB) domain. Group 1 PAK kinases (PAK1, 2 and 3) regulate the activity of an adjacent conserved autoinhibitory domain and are associated with cellular processes, including cytoskeleton rearrangement, apoptosis and MAP kinase signalling. Group 2 PAKs (PAK4, 5, and 6) lack the autoinhibitory domain and are not activated by Cdc42/Rac binding.
PAK2 has a cytostatic effect on cells and is activated in response to cellular stresses such hyperosmolarity, serum starvation, contact inhibition and DNA damage from radiation and chemicals. Unlike other PAKs, PAK2 can be activated by proteolytic cleavage to generate a constitutively active fragment, PAK2p34, which induces a cell death response. This induction is thought to be regulated by Rho GTPase-activating protein 10 which inhibits the protein kinase activity of PAK2p34 and causes it to localise to the perinuclear region instead of the nucleus. PAK2 may also play a role in X-linked mental retardation.
Rabbit anti Human PAK2 antibody detects p21-activated kinase-2 as a single a band of 58 kDa in a range of human cell line lysates.
- Target Species
- Western Blotting
- Rabbit anti PAK2 detects a band of approximately 58 kDa in MCF7 cell lysates.
- Product Form
- Purified IgG - liquid
- Rabbit polyclonal antibody purified by affinity chromatography
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
- 0.09% Sodium Azide (NaN3)
- 14 amino acid peptide sequence near the carboxy terminus of human PAK2.
- Store undiluted at -20oC, avoiding repeated freeze thaw cycles.
- 12 months from date of despatch
- Entrez Gene
- GO Terms
- GO:0005886 plasma membrane
- GO:0005829 cytosol
- GO:0004674 protein serine/threonine kinase activity
- GO:0005524 ATP binding
- GO:0005634 nucleus
- GO:0006469 negative regulation of protein kinase activity
- GO:0006921 cellular component disassembly involved in apoptosis
- GO:0007411 axon guidance
- GO:0042802 identical protein binding
- GO:0016032 viral reproduction
- GO:0042981 regulation of apoptosis
- GO:0018105 peptidyl-serine phosphorylation
- GO:0019901 protein kinase binding
- GO:0030296 protein tyrosine kinase activator activity
- GO:0031295 T cell costimulation
- GO:0040008 regulation of growth
- GO:0044419 interspecies interaction between organisms
- GO:0046777 protein autophosphorylation
- GO:0048471 perinuclear region of cytoplasm
- GO:0050690 regulation of defense response to virus by virus
- GO:0050731 positive regulation of peptidyl-tyrosine phosphorylation
- GO:0050852 T cell receptor signaling pathway
- PrecisionAb is a trademark of Bio-Rad Laboratories.
- For research purposes only
Applications of PAK2 antibody
|Application Name||Verified||Min Dilution||Max Dilution|
|Immunohistology - Paraffin 1|
- 1 This product requires antigen retrieval using heat treatment prior to staining of paraffin sections. Sodium citrate buffer pH 6.0 is recommended for this purpose.
The PrecisionAb label is reserved for antibodies that meet the defined performance criteria within Bio-Rad's ongoing antibody validation programme. Click here to learn how we validate our PrecisionAb range. Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Further optimization may be required dependent on sample type.
Secondary Antibodies Available
|Description||Product Code||Applications||Pack Size||List Price||Quantity|
|Goat anti Rabbit IgG (H/L):HRP||STAR208P||WB||2 ml|
Product Specific References
Roig, J. & Traugh, J.A. (2001) Cytostatic p21 G protein-activated protein kinase gamma-PAK.
Vitam Horm. 62: 167-98.
Rudel, T. & Bokoch, G.M. (1997) Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2.
Science. 276 (5318): 1571-4.
Jaffer, Z.M. & Chernoff, J. (2002) p21-activated kinases: three more join the Pak.
Int J Biochem Cell Biol. 34 (7): 713-7.
Thome, M. et al. (1997) Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors.
Nature. 386 (6624): 517-21.
Irmler, M. et al. (1997) Inhibition of death receptor signals by cellular FLIP.
Nature. 388 (6638): 190-5.
Shu, H.B. et al. (1997) Casper is a FADD- and caspase-related inducer of apoptosis.
Immunity. 6 (6): 751-63.
Hu, S. et al. (1997) I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1- and CD-95-induced apoptosis.
J Biol Chem. 272 (28): 17255-7.
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