|Application ||WB, E|
|Other Accession||NP_619579, 1073|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||18737 Da|
|Other Names||Cofilin-2, Cofilin, muscle isoform, CFL2|
|Format||0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Goat Anti-Cofilin 2 (muscle) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods (By similarity).|
|Cellular Location||Nucleus matrix. Cytoplasm, cytoskeleton|
|Tissue Location||Isoform CFL2b is expressed predominantly in skeletal muscle and heart. Isoform CFL2a is expressed in various tissues|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes an intracellular protein that is involved in the regulation of actin-filament dynamics. This protein is a major component of intranuclear and cytoplasmic actin rods. It can bind G- and F-actin in a 1:1 ratio of cofilin to actin, and it reversibly controls actin polymerization and depolymerization in a pH-dependent manner. Mutations in this gene cause nemaline myopathy type 7, a form of congenital myopathy. Alternative splicing results in multiple transcript variants.
Muscle LIM protein interacts with cofilin 2 and regulates F-actin dynamics in cardiac and skeletal muscle. Papalouka V, et al. Mol Cell Biol, 2009 Nov. PMID 19752190.
Cofilin activation in peripheral CD4 T cells of HIV-1 infected patients: a pilot study. Wu Y, et al. Retrovirology, 2008 Oct 17. PMID 18928553.
Nemaline myopathy with minicores caused by mutation of the CFL2 gene encoding the skeletal muscle actin-binding protein, cofilin-2. Agrawal PB, et al. Am J Hum Genet, 2007 Jan. PMID 17160903.
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, et al. Cell, 2006 Nov 3. PMID 17081983.
Cofilin cross-bridges adjacent actin protomers and replaces part of the longitudinal F-actin interface. Kudryashov DS, et al. J Mol Biol, 2006 May 5. PMID 16530787.
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