ACTN1 forms an antiparallel homodimer, with each monomer containing an actin-binding domain at the amino terminus. This structure allows ACTN1 to interact with a variety of proteins involved in cellular adhesion, migration, and immune cell targeting . The protein is essential for maintaining the cytoskeleton’s stability and facilitating cellular processes such as motility and signal transduction.
There are four distinct isoforms of ACTN1, resulting from alternative splicing. These isoforms exhibit different tissue expression patterns, with some being specific to muscle tissues and others found in non-muscle cells . The muscle isoforms, ACTN2 and ACTN3, localize to the Z-discs of striated muscle and to dense bodies and plaques in smooth muscle. In contrast, the non-muscle isoforms, ACTN1 and ACTN4, are present in stress fibers, sites of adhesion, intercellular contacts, filopodia, and lamellipodia .
The mouse anti-human ACTN1 antibody is typically produced by immunizing mice with a synthetic peptide corresponding to the carboxy-terminal residues of human ACTN1. The resulting polyclonal antibodies are then purified using antigen affinity chromatography . This antibody is highly specific and can detect endogenous levels of total ACTN1 protein in various species, including humans, mice, and rats .
The mouse anti-human ACTN1 antibody is widely used in research for various applications, including Western blotting, immunofluorescence, and immunocytochemistry . It is particularly useful for studying the role of ACTN1 in cellular processes and for investigating the protein’s interactions with other cytoskeletal components.