Reactive species
Human, Mouse,Rat
Antibody type
Monoclonal antibodies
Protein name
LIM domain kinase 1 (LIMK-1) (EC 2.7.11.1)
Immunogen
Synthesized peptide derived from human LIMK-1/2
Specificity
This antibody detects endogenous levels of LIMK-1/2 at Human, Mouse,Rat
Constitute
PBS, pH7.4, 50% glycerol, 0.03%Proclin 300
Source
Mouse,monoclonal:IgG1,Lambda
Dilution rate
WB 1:500-2000 ELISA 1:5000-20000
Purification process
Protein G
Other name
LIM domain kinase 1 (LIMK-1) (EC 2.7.11.1)
Background
LIM domain kinase 1(LIMK1) Homo sapiens There are approximately 40 known eukaryotic LIM proteins, so named for the LIM domains they contain. LIM domains are highly conserved cysteine-rich structures containing 2 zinc fingers. Although zinc fingers usually function by binding to DNA or RNA, the LIM motif probably mediates protein-protein interactions. LIM kinase-1 and LIM kinase-2 belong to a small subfamily with a unique combination of 2 N-terminal LIM motifs and a C-terminal protein kinase domain. LIMK1 is a serine/threonine kinase that regulates actin polymerization via phosphorylation and inactivation of the actin binding factor cofilin. This protein is ubiquitously expressed during development and plays a role in many cellular processes associated with cytoskeletal structure. This protein also stimulates axon growth and may play a role in brain development. LIMK1 hemizygosity is implicated in the impaired visuospatial constructive cog
Function
catalytic activity:ATP + a protein = ADP + a phosphoprotein.,disease: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.,function:Protein kinase which regulates actin filament dynamics. Phosphorylates and inactivates the actin binding/depolymerizing factor cofilin, thereby stabilizing the actin cytoskeleton. Isoform 3 has a dominant negative effect on actin cytoskeletal changes. May be involved in brain development.,PTM:Autophosphorylated.,PTM:Phosphorylated on serine and/or threonine residues by ROCK1. May be dephosphorylated and inactivated by SSH1.,similarity:Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.,similarity:Contains 1 PDZ (DHR) doma
