Recombinant Proteins
Product List
CFL1 Human
Cofilin-1 Human Recombinant
CFL2 Human
Cofilin-2 Human Recombinant
CFL2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
Cofilin is a member of the actin-depolymerizing factor (ADF)/cofilin family of proteins, which are small actin-binding proteins that play a crucial role in the regulation of actin dynamics. These proteins are involved in the rapid depolymerization of actin microfilaments, contributing to the dynamic instability of actin filaments . In humans and mice, three highly conserved genes encode cofilin: CFL1 (non-muscle cofilin), CFL2 (muscle cofilin), and DSTN (destrin or ADF) .
Cofilin is a low molecular weight protein (~21 kDa) that is ubiquitously expressed in all vertebrates . It is found in various tissues, with specific isoforms showing distinct expression patterns. For instance, CFL1 is predominantly expressed in non-muscle tissues, while CFL2 is primarily found in muscle tissues . Cofilin’s key biological properties include its ability to bind to both monomeric (G-actin) and filamentous actin (F-actin), with a preference for ADP-actin over ATP-actin .
Cofilin plays a pivotal role in regulating actin dynamics by severing actin filaments and enhancing their depolymerization . This activity is essential for various cellular processes, including cell motility, muscle contraction, and transcription regulation . In the immune system, cofilin is involved in immune responses and pathogen recognition by modulating the actin cytoskeleton, which is crucial for the migration and function of immune cells .
Cofilin exerts its effects by binding to actin filaments and inducing conformational changes that promote filament severing and depolymerization . It interacts with various binding partners, including actin-interacting protein 1 (Aip1) and the Arp2/3 complex, to regulate actin dynamics . Cofilin’s activity is modulated by phosphorylation at serine 3, which inhibits its binding to actin and thus its actin-severing activity . Additionally, cofilin is involved in downstream signaling cascades, such as the NF-kB and JNK pathways, which are activated in response to cellular stress .
The expression and activity of cofilin are tightly regulated by multiple mechanisms. Transcriptional regulation involves various transcription factors that control the expression of cofilin genes . Post-translational modifications, such as phosphorylation, play a critical role in modulating cofilin’s activity. Phosphorylation at serine 3 by LIM kinases inhibits cofilin’s actin-binding ability, while dephosphorylation by slingshot phosphatases activates it . Other regulatory mechanisms include pH changes and interactions with phosphatidylinositol (4,5)-bisphosphate .
Cofilin has significant applications in biomedical research, particularly in the study of cancer metastasis and neurodegenerative diseases . Its role in actin dynamics makes it a potential target for therapeutic strategies aimed at modulating cell motility and invasion. Cofilin inhibitors and gene therapy approaches are being explored for their potential to treat diseases characterized by cofilin dysregulation . Additionally, cofilin’s involvement in cellular processes makes it a valuable diagnostic tool for various diseases .
Cofilin plays a crucial role throughout the life cycle, from development to aging and disease . During development, cofilin is essential for processes such as cell migration, tissue morphogenesis, and organ formation . In adulthood, cofilin continues to regulate actin dynamics, contributing to tissue homeostasis and repair . Dysregulation of cofilin activity is associated with various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases . Understanding cofilin’s role in these processes provides insights into its potential as a therapeutic target.
