|Other Names||LIM domain kinase 1, LIMK-1, LIMK1, LIMK|
|Target/Specificity||The synthetic peptide sequence is selected from aa 9~25of human LIMK1.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop. LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin- 2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and stabilizing the actin cytoskeleton. In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation. Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly. Stimulates axonal outgrowth and may be involved in brain development. Isoform 3 has a dominant negative effect on actin cytoskeletal changes. Required for atypical chemokine receptor ACKR2-induced phosphorylation of cofilin (CFL1).|
|Cellular Location||Cytoplasm. Nucleus. Note=Predominantly found in the cytoplasm|
|Tissue Location||Highest expression in both adult and fetal nervous system. Detected ubiquitously throughout the different regions of adult brain, with highest levels in the cerebral cortex. Expressed to a lesser extent in heart and skeletal muscle|
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LIMK1, a member of the Ser/Thr protein kinase family, may be a component of an intracellular signaling pathway and may be involved in brain development. It phosphorylates and inactivates the actin binding/depolymerizing factor cofilin and induces actin cytoskeletal changes. The LIM domain interacts with the cytoplasmic domain of NRG1, and this cytoplasmic protein also binds ROCK1, whic phosphorylates LIMK1 on serine and/or threonine residues. Highest expression occurs in both adult and fetal nervous systems. It is detected ubiquitously throughout the different regions of adult brain, with highest levels in the cerebral cortex, and is expressed to a lesser extent in heart and skeletal muscle. Haploinsufficiency of LIMK1 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in Williams-Beuren syndrome (WBS), a rare developmental disorder. It is a contiguous gene deletion syndrome involving genes from chromosome band 7q11.23. This protein contains 2 LIM zinc-binding domains and 1 PDZ/DHR domain.
Ohashi, K., et al., J. Biol. Chem. 275(5):3577-3582 (2000).Maekawa, M., et al., Science 285(5429):895-898 (1999).Edwards, D.C., et al., J. Biol. Chem. 274(16):11352-11361 (1999).Osborne, L.R., et al., Genomics 36(2):328-336 (1996).Frangiskakis, J.M., et al., Cell 86(1):59-69 (1996).
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