Serine/Threonine-Protein Kinase PAK 1 (PAK1) Human Recombinant Protein

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 chokine 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 chokine uptake and degradation. In synapses, ses to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation

Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway.Brown J.L., Stowers L., Baer M., Trejo J., Coughlin S., Chant J.Curr. Biol. 6:598-605(1996) Human p21-activated kinase (Pak1)regulates actin organization in mammalian cells.Sells M.A., Knaus U.G., Bagrodia S., Ambrose D.M., Bokoch G.M., Chernoff J.Curr. Biol. 7:202-210(1997) Human PAK1B.Reid T., Aspenstroem P., Bertoglio J.Human chromosome 11 DNA sequence and analysis including novel gene identification.Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.Nature 440:497-500(2006) Pak1 phosphorylation of snail, a master regulator of epithelial-to-mesenchyme transition, modulates snail's subcellular localization and functions.Yang Z., Rayala S., Nguyen D., Vadlamudi R.K., Chen S., Kumar R.Cancer Res. 65:3179-3184(2005) Integrin engagement differentially modulates epithelial cell motility by RhoA/ROCK and PAK1.Zhou H., Kramer R.H.J. Biol. Chem. 280:10624-10635(2005) Essential role of CIB1 in regulating PAK1 activation and cell migration.Leisner T.M., Liu M., Jaffer Z.M., Chernoff J., Parise L.V.J. Cell Biol. 170:465-476(2005) p21-activated kinase 1 regulates microtubule dynamics by phosphorylating tubulin cofactor B.Vadlamudi R.K., Barnes C.J., Rayala S., Li F., Balasenthil S., Marcus S., Goodson H.V., Sahin A.A., Kumar R.Mol. Cell. Biol. 25:3726-3736(2005) A probability-based approach for high-throughput protein phosphorylation analysis and site localization.Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.Nat. Biotechnol. 24:1285-1292(2006) CRIPak, a novel endogenous Pak1 inhibitor.Talukder A.H., Meng Q., Kumar R.Oncogene 25:1311-1319(2006) JAK2 tyrosine kinase phosphorylates PAK1 and regulates PAK1 activity and functions.Rider L., Shatrova A., Feener E.P., Webb L., Diakonova M.J. Biol. Chem. 282:30985-30996(2007) Identification of phosphorylation sites in betaPIX and PAK1.Mayhew M.W., Jeffery E.D., Sherman N.E., Nelson K., Polefrone J.M., Pratt S.J., Shabanowitz J., Parsons J.T., Fox J.W., Hunt D.F., Horwitz A.F.J. Cell Sci. 120:3911-3918(2007) Affixin activates Rac1 via betaPIX in C2C12 myoblast.Matsuda C., Kameyama K., Suzuki A., Mishima W., Yamaji S., Okamoto H., Nishino I., Hayashi Y.K.FEBS Lett. 582:1189-1196(2008) Scrib regulates PAK activity during the cell migration process.Nola S., Sebbagh M., Marchetto S., Osmani N., Nourry C., Audebert S., Navarro C., Rachel R., Montcouquiol M., Sans N., Etienne-Manneville S., Borg J.-P., Santoni M.-J.Hum. Mol. Genet. 17:3552-3565(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011)

Small volumes of PAK1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

MBS1467079 is a recombinant protein targeting PAK1. Also known as Recombinant Human Serine/threonine-protein kinase PAK 1. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.