Actin Antibody

Actin Antibody Available at Imgenex now Actin is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton. It is the monomeric subunit of microfilaments, one of three main components of the cytoskeleton, and thin filaments that are part of the contractile apparatus of muscle cells. It is the most abundant protein in eukaryotic cells typically representing about 15% in some cell types. The protein is highly conserved, and forms a huge variety of structure in cells together with a large number of actin binding proteins. Actin filaments with myosin interact to produce an effect of slip, which is the basis of muscle contraction and many aspects of cell motility, including cytokinesis. The individual units of actin are known as globular actin (G-actin), which brings together in long filaments called polymers F-actin. Two F-actin parallel strands twist around each other in a helical formation, giving rise to microfilaments of the cytoskeleton. Microfilaments approximately 7 nm in diameter with a loop of helix repeating every 37nm. Each protômero actin binds an ATP molecule and has a high affinity site for both calcium ions and magnesium, as well as several low affinity sites. It exists as a monomer to salt in low concentrations, but filaments form rapidly with increasing salt concentration, with the consequent hydrolysis of ATP. Actin from many sources forms a tight complex with deoxyribonuclease (DNase I), although the significance of this remains unknown. The formation of this complex results in the inhibition of DNase I and actin loses its ability to polymerize. It has been shown that an actin ATPase domain shares similarity with ATPase domains of hexokinase and hsp70 proteins. In vertebrates there are three groups of actin isoforms: alpha, beta and gamma. The actin are found in muscle tissues and are an important component of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility. SBM, a major component of bacterial cytoskeleton, exhibits high structural homology to its counterpart eukaryotic actin. Moreover, it was suggested that members of the Rho family of small guanosine triphosphatases have emerged as key regulators of the actin cytoskeleton, and through its interaction with target proteins, which ensure the coordinated control of other cellular activities such as gene transcription and Accession