|Application ||WB, IHC-P, IF, E|
|Other Accession||NP_002568, 32483399|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||58043 Da|
|Application Notes||PAK2 antibody can be used for the detection of PAK2 by Western blot at 0.5 - 2 µg/mL. Antibody can also be used for immunohistochemistry starting at 10 µg/mL. For immunofluorescence start at 20 µg/mL.|
|Other Names||PAK2 Antibody: PAK65, PAKgammaGamma-PAK, PAK-2, p21 protein (Cdc42/Rac)-activated kinase 2|
|Reconstitution & Storage||PAK2 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||PAK2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Full-length PAK2 stimulates cell survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Phosphorylates JUN and plays an important role in EGF- induced cell proliferation. Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP. Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis. On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway. Caspase- activated PAK2 phosphorylates MKNK1 and reduces cellular translation.|
|Cellular Location||Serine/threonine-protein kinase PAK 2: Cytoplasm. Note=MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane|
|Tissue Location||Ubiquitously expressed. Higher levels seen in skeletal muscle, ovary, thymus and spleen|
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Provided below are standard protocols that you may find useful for product applications.
PAK2 Antibody: The p21-activated kinases (PAKs) are serine-threonine kinases that bind to the active forms of Cdc42 and Rac. They are divided into two groups, the first of which include PAK1, 2 and 3, and can be activated by Cdc42/Rac binding. Group 1 PAKs contain an autoinhibitory domain whose activity is regulated by Cdc42/Rac binding. The group 1 PAKs are known to be involved in cellular processes such as gene transcription, apoptosis, and cell morphology and motility. Much less is known about the second group, which includes PAK4, 5 and 6, and are not activated by Cdc42/Rac binding. Of the six PAK proteins, only PAK2 is ubiquitously expressed and cleaved by caspase-3. This cleavage removes the amino-terminal regulatory domain and generates a constitutively active kinase fragment. Recent experiments have shown that following cleavage, the active fragment is myristoylated and directed to the plasma membrane and membrane ruffles where it promotes cell death via increased signaling through the c-Jun N-terminal kinase pathway, but without compromising mitochondrial integrity.
Jaffer ZM and Chernoff J. p21-activated kinases: three more join the Pak. Int. J. Biochem. Cell Biol. 2002; 34:713-7.
Rudel T and Bokoch GM. Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science 1997; 276:1571-4.
Vilas GL, Corvi MM, Plummer GJ, et al. Posttranslational myristoylation of caspase-activated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events. Proc. Natl. Acad. Sci. USA 2006; 103:6542-7.
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