|Other Names||LIM domain kinase 2, LIMK-2, LIMK2|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP7814a was selected from the N-term region of human LIMK2B . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|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||Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro.|
|Cellular Location||Isoform LIMK2a: Cytoplasm. Nucleus. Note=Isoform LIMK2a is distributed in the cytoplasm and the nucleus|
|Tissue Location||Highest expression in the placenta; moderate level in liver, lung, kidney, and pancreas. LIMK2a is found to be more abundant then LIMK2b in liver, colon, stomach, and spleen, while in brain, kidney, and placenta LIMK2b is the dominant form In adult lung, both LIMK2a and LIMK2b is nearly equally observed|
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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. The LIMK2 protein is phosphorylated and activated by ROCK, a downstream effector of Rho, and LIM kinase 2, in turn, phosphorylates cofilin, inhibiting its actin-depolymerizing activity. It is thought that this pathway contributes to Rho-induced reorganization of the actin cytoskeleton. Two alternative splice variants of LIMK2 that utilize alternative promoters have been identified.
Blume-Jensen P, et al. Nature 2001. 411: 355.Cantrell D, J. Cell Sci. 2001. 114: 1439.Jhiang S Oncogene 2000. 19: 5590.Manning G, et al. Science 2002. 298: 1912.Moller, D, et al. Am. J. Physiol. 1994. 266: C351-C359.Robertson, S. et al. Trends Genet. 2000. 16: 368.Robinson D, et al. Oncogene 2000. 19: 5548.Van der Ven, P, et al. Hum. Molec. Genet. 1993. 2: 1889.Vanhaesebroeck, B, et al. Biochem. J. 2000. 346: 561.Van Weering D, et al. Recent Results Cancer Res. 1998. 154: 271.
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