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Phone (800) 975-6866 / (413) 477-6866 • FAX (413) 643-0067 •


SKU: FC0104
LIM domain kinase 2

Above: WB 1:500 with THP-1 cell lysate.  Apparent MW is around 76 kDa appearing as a doublet.

Below: IHC 1:50 with FFPE mouse liver showing DBA staining (brown) and Hematoxylin QS counterstaining (blue)





Host Species: 
Synthetic peptide from human LIMK-2 within amino acids 570-638.  The peptide is conserved in several other species.  The selected peptide was post-synthetically modified before coupling to carrier protein.
Reactive Species: 
Highly conserved suggesting multiple species
Affinity purified IgY. This antibody can be conjugated to fluorophores and other secondary enzymes as an additional service.
Buffer & Formulation: 
0.5 mg/ml in antibody stabilization buffer
Aliquot and freeze at -20° C. Avoid freeze-thaw cycles.


Western Blotting: 
Not tested
Flow Cytometry: 
Not tested

The LIMK2 gene spans 68,617 base pairs, comprising of 19 potential exons. To date, LIM kinase homologues have been identified in a variety of species including; humans, mice, rats and chickens. LIM kinases (LIMKs) are important cell cytoskeleton regulators that play a prominent role in cancer manifestation and neuronal diseases(1). The LIMK family consists of two homologues, LIMK1 and LIMK2, which differ from one another in expression profile, intercellular localization, and function(1).  They are dual-specificity kinases, phosphorylating both serine/threonine and tyrosine residues(1). Both are ubiquitous and are expressed in various tissues(1). They share 50% homology in amino-acid sequence, with higher conservation in specific domains (e.g. 70% sequence homology in the kinase domain). Their expression patterns, however, are different: LIMK1 is expressed mainly in embryonic brain tissue and heart(1), whereas LIMK2 is expressed in all tissues(1). They also have different subcellular localizations: whereas LIMK1 is mainly localized to the focal adhesion site, LIMK2 is found throughout the cytoplasm and in association with the cis-Golgi compartment(1). 

There is emerging evidence that each may be subject to different regulatory pathways and may contribute to both distinct and overlapping cellular and developmental functions(2). Normal central nervous system development is reliant upon the presence of LIMK1, and its deletion has been implicated in the development of the human genetic disorder Williams syndrome(2). Normal testis development, on the other hand, is disrupted by the deletion of LIMK2(2). In addition, the possible involvement of each kinase in cardiovascular disorders as well as cancer has emerged(2). The LIM kinases have been proposed to play an important role in tumour-cell invasion and metastasis; fine-tuning the balance between phosphorylated and non-phosphorylated cofilin may be a significant determinant of tumour-cell metastatic potential(2). LIMKs have become persuasive targets for drug design as their inhibition increases active unphosphorylated cofilin, inhibits cancer metastasis and development, and shows promise as a possible therapeutic measure for LIMK-induced diseases(1). More information at UniProtKB#P53671



1.  Roni Rak1, Roni Haklai1, Galit Elad-Tzfadia1, Haim J. Wolfson2, Shmuel Carmeli3 and Yoel Kloog1.  Novel LIMK2 inhibitor blocks Panc-1 tumor growth in a mouse xenograft model. Oncoscience 2014, Vol.1, No.1, pp 39-48.

2.  Rebecca W. Scott, Michael F. Olson. LIM kinases: function, regulation and association with human disease. Journal of Molecular Medicine, June 2007, Volume 85, Issue 6, pp 555-568.

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