Anti-Actin Antibody, clone C4, Alexa Fluor(R) 555 Conjugate clone C4, from mouse, ALEXA FLUOR(R) 647

Actins are ubiquitous eukaryotic proteins that serve as a multi-functional, basic building blocks of cytoskeletal microfilaments. They play critical roles in a wide range of cellular processes, including cell division, cell migration, chromatin remodeling, trascriptional regulation and vesicle trafficking. These funstions are attributed to their ability to form filaments, which can quickly assemble and disassemble depending upon the needs of the cell. At least six different actin types have been reported in mammals. Although actins show about 90% overall sequence homology, isoforms do not show spatial, temporal and tissue-specific expression patterns and only 50-60% homology is found in their 18 N-terminal residues. Beta and gamma-actins, also known as cytoplasmic actins, are highly conserved in higher animals and are predominantly expressed in non-muscle cells where they control cell structure. Exocytosis, and motility. They are nearly identical proteins and differ only in four amino acids at the N-terminal region. The other four actin isoforms are typically found in specific adult muscle tissue types. Alpha-cardiac and alpha-skeletal actins are expressed in striated cardiac and skeletal muscles, respectively. Alpha and gamma actins are primarily found in vascular smooth muscle and enteric smooth muscles, respectively. It has been shown that under calcium-bound conditions, beta-actin exhibits more dynamic behavior than gamma-actin with higher rates of polymerization and depolymerization. Also, beta- and gamma-actins can readily copolymerize, and the resulting filaments exhibit polymerization and depolymerization rates that vary depending on the ration of beta- to gamma-actin (Lessard, JL.,et al.(1988). Cell Motility Cytoskeleton 10(3); 349-362.