CFL2 Human

Cofilin-2, also known as CFL2, is a member of the cofilin family of actin-binding proteins. This family includes cofilin-1 (CFL1) and destrin (DSTN), all of which play crucial roles in the regulation of actin filament dynamics . Cofilin-2 is specifically expressed in skeletal muscle tissue and is essential for muscle function and development .

Cofilin-2 is encoded by the CFL2 gene located on chromosome 14 in humans . The protein consists of 166 amino acids and has a molecular weight of approximately 20.4 kDa . It shares significant homology with other members of the cofilin family, particularly in regions responsible for actin-binding .

Cofilin-2 is an actin-modulating protein that binds to filamentous F-actin and depolymerizes it, inhibiting the polymerization of monomeric G-actin in a pH-dependent manner . This activity is crucial for the dynamic reorganization of the actin cytoskeleton, which is essential for various cellular processes, including cell motility, division, and muscle contraction .

Recombinant human cofilin-2 is typically produced in Escherichia coli (E. coli) expression systems . The recombinant protein is often tagged with a His-tag to facilitate purification and is lyophilized for storage and transport . The purity of the recombinant protein is usually greater than 90%, making it suitable for various research applications .

Mutations in the CFL2 gene are associated with nemaline myopathy, a muscle disorder characterized by muscle weakness and the presence of rod-like structures called nemaline bodies in muscle fibers . Deficiency of cofilin-2 can lead to reduced depolymerization of actin filaments, causing their accumulation and contributing to the pathology of the disease .

Recombinant human cofilin-2 is widely used in research to study actin dynamics, muscle physiology, and related disorders. It is also used in biochemical assays to investigate the mechanisms of actin filament depolymerization and the effects of various regulatory proteins on actin dynamics .