Anti-PAK2

In 1X PBS, pH 7.4, with 0.09% sodium azide. PAK2, a member of the STE20 subfamily of Ser/Thr protein kinases, acts on a variety of targets. It phosphorylates ribosomal protein S6, histone H4 and myelin basic protein. PAK2 interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1. Expression is ubiquitous, with higher levels seen in skeletal muscle, ovary, thymus and spleen. PAK2 is autophosphorylated when activated by CDC42/p21. The protein structure contains 1 CRIB domain. Protein 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. [The UniProt Consortium]