Monoclonal mouse anti-actin antibody was used as a loading control for western blot analysis of immunoprecipitated proteins from rat dorsal root ganglion cocultures.
Cardiac myocytes were stained with monoclonal mouse anti-actinin to visualize the Z-lines after fixation in pre-cooled methanol/acetone mix (1:1) for 10 minutes at 4 °C.
Monoclonal Anti-α-Sarcomeric Actin (mouse IgM isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. Actin is one of the most conserved eukaryotic proteins and the isoforms show >90% overall sequence homology. It is expressed in mammals and birds as six isoforms. Four of the six represent differentiation markers of muscle tissues. The other two are found in practically all cells.
Actin is a cytoskeletal protein that regulates cell motility, secretion, phagocytosis and cytokinesis. The NH2-terminal of actin may function as antigen. This terminal may also modulate actin interactions and may associate with proteins such as myosin.
