Actin

Duchenne muscular dystrophy (DMD) is a severe muscle wasting condition, causing disability and early death. There is currently no cure or adequate treatment for DMD, but pioneering research indicates that injection of a laminin protein may prevent (or at least slow) this muscle degeneration.

Actin is a ubiquitous and an essential component of the cytoskeleton, with critical roles in a wide range of cellular processes. It is abundant protein whose monomers polymerize into polarized actin filaments, within epithelial cells. Filamentous actin is concentrated at the plasma membrane where a wide variety of actin-associated proteins harness the potential and structure of actin filaments to moderate functions at the plasma membrane (1).

Actins are an essential component of the cytoskeleton, with critical roles in a wide range of cellular processes, including cell migration, division, and regulation of gene expression. These functions are attributed to the ability of actin to form filaments that can rapidly assemble and disassemble according to the needs of the cell. There exist six different but highly conserved actin isoforms in vertebrates (1).

Actins are highly conserved, commonly found and abundant proteins involved in several types of cell motility as well as cytoskeleton maintenance. In vertebrate species, three main groups of actin isoforms, the alpha, beta and gamma, have been identified. Alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus.

Myosin is a super family of actin based molecular motors that hydrolyze ATP and generate physical force to move specific molecules inside the cell. This super family, divided into at least twenty four classes based on head domain sequence similarity and domain organization^. The processivity of myosins along an actin filament and transport of intracellular ‘cargo’ are achieved by generating physical force from chemical energy of ATP followed by appropriate conformational changes (1).

A growing body of data and studies using actin antibodies supports a view of the actin cytoskeleton of smooth muscle cells as a dynamic structure that plays an integral role in regulating the development of mechanical tension and the material properties of smooth muscle tissues.

The loading controls on our antibody database are widely used in gel electrophoresis and Western blotting studies. Products like the GAPDH antibody detect "housekeeping" proteins which are abundantly distributed in cells. This makes them useful for checking the even loading of gel samples, and the even transfer of proteins at the blotting stage. They also serve a purpose in quality control, by verifying reagents are working correctly, and in the standardization of experimental results.

Profilin-1, or Pfn-1, is a small actin-binding protein which plays an essential role controlling the growth of microfilaments. Profilin 1 and Profilin 2 have similar biochemical properties but are expressed in different tissues. The Profilin 1 antibody targets the more common form of the protein, which is expressed everywhere but the skeletal muscle. We at Novus Biologicals have an extensive range of Profilin I and Profilin II antibody products in our antibody catalog.

A highly conserved, abundant protein found in practically all eukaryotic cells, actin is a monomeric subunit of skeletal muscle thin filaments, and cytoskeleton microfilaments. Actin antibody products are routinely used in cell marker and loading control assays. However, actin antibody reagents are also used for cytoskeleton, cell motility, cytokinesis and cell signalling research.

One of six actin isoforms so far identified, beta actin is a highly conserved cytoskeletal protein involved in cell structure, motility, and cohesion. We at Novus Biologicals have many different beta-actin products in our catalog, used in areas such as cytoskeleton and signal transduction research. They are also used as loading controls in protein assays. Beta-actin is known as a “housekeeping” protein, i.e.