|Application ||WB, IHC, IF|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||60647 Da|
|Other Names||Serine/threonine-protein kinase PAK 1, Alpha-PAK, p21-activated kinase 1, PAK-1, p65-PAK, PAK1|
|Target/Specificity||A synthetic peptide corresponding to residues in the human PAK1 protein was used as immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PAK1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus. In podocytes, promotes NR3C2 nuclear localization. Required for atypical chemokine receptor ACKR2- induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F- actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation. Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion (PubMed:25766321).|
|Cellular Location||Cytoplasm. Cell junction, focal adhesion. Cell membrane. Cell projection, ruffle membrane. Cell projection, invadopodium. Note=Colocalizes with RUFY3, F- actin and other core migration components in invadopodia at the cell periphery (PubMed:25766321). Recruited to the cell membrane by interaction with CDC42 and RAC1. Recruited to focal adhesions upon activation. Colocalized with CIB1 within membrane ruffles during cell spreading upon readhesion to fibronectin|
|Tissue Location||Overexpressed in gastric cancer cells and tissues (at protein level) (PubMed:25766321)|
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Provided below are standard protocols that you may find useful for product applications.
p21-activated kinase 1 (PAK1) is a member of a family of serine/threonine protein kinase defined by their interaction with the small GTPases, Cdc42 and Rac (1-2). The PAK proteins can be essentially divided into two categories, groups I (PAK1, PAK2 and PAK3) and group II (PAK4, PAK5 and PAK6), based on their structures (3). PAK1 participates in regulating the actin cytoskeleton, focal adhesion contacts, cell motility, apoptosis and transcription. It also promotes the disassembly of stress fibers (4-5). PAK1 also binds PIX (PAK-binding protein), COOL and adapter protein Nck (5).
1. Manser, E., Leung, T., Salihuddin, H., Zhao, Z., and Lim, L. (1994) Nature 363, 364
2. Daniels, R. H., and Bokoch, G. M. (1999) Trends Biochem. Sci. 24, 350
3. Jaffer, Z. M., and Chernoff, J. (2002) Int. J. Biochem. Cell Biol. 34, 713-717.
4. Sanders, L. C.; Matsumura, F.; Bokoch, G. M.; de Lanerolle, P. : Science 283: 2083-2085, 1999.
5. Sells, M.A., Boyd, J.T. and Chernoff, J., 1999. J. Cell Biol. 145, pp. 837
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