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Actin antibodies available now in Imgenex
Actin antibodies available now in Imgenex
Actin is a ubiquitous protein involved in the formation of filaments that are key components of the cytoskeleton. It is the monomeric subunit of microfilaments, one of the three major components of the cytoskeleton, and thin filaments that are part of the contraction mechanism in muscle cells.
It is most abundant in the typical eukaryotic cell, about 15% in some cell types. The protein is highly conserved, and forms a vast body of cells in concert with a large number of actin binding proteins. Actin filaments interact with myosin to produce a slippery effect, which is the basis of many aspects of muscle contraction and cell motility, including cytokinesis.
Individual subunits of actin are found as spherical actin (G-actin) combining in long filamentous polymers called F-actin. The two parallel F-actin strands fold into a helical formation around each other, giving rise to microfilaments of the cytoskeleton. The microfilament measures approximately 7 nm in diameter with a loop of helix repeating every 37nm. Each actin protomer binds one molecule of ATP and has a high affinity site for calcium or magnesium ions, as well as several low affinity sites. It exists as a monomer at low salt concentrations, but the filaments rapidly increase as the salt concentration increases, with ATP resulting in hydrolysis. Actin from many sources forms a tight complex with deoxyribonuclease (DNase I), although the importance of this is still unknown.
This complex results in inhibition of DNase I activity, and loses its ability to polymerize actin. It has been shown that the ATPase domain of actin shares similarity with the ATPase domain of hexokinase and Hsp70 protein. There are three groups of actin isoforms in vertebrates: alpha, beta, and gamma. Alpha actin is found in muscle tissue and is a major component of the contraction mechanism. Beta and gamma actin are present as components of the cytoskeleton in most cell types and as mediators of internal cell motility.
MreB, a major component of the bacterial cytoskeleton, exhibits high structural homology to its eukaryotic counterpart actin. Furthermore it has been suggested that members of the Rh family of small guanosine trifosphatases have emerged as key regulators of the actin cytoskeleton, and that through their interactions with several target proteins, they are involved in gene transcription and other cellular activities such as adhesion. To ensure coordinated control of
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