Product Uses
Measurement of F-actin activated myosin ATPase activity
Identification/characterization of proteins or small molecules that affect myosin ATPase activity
Identification/characterization of proteins or small molecules that affect myosin / F- actin interaction
Materials
Skeletal muscle myosin protein has been purified from rabbit psoas muscle (1, 2). The full length myosin protein was purified with its essential light chains (ELC) and regulatory light chains (RLC), see Figure 1 and 2. Myosin was then digested with alpha-chymotrypsin to liberate the soluble subfragment-1 (S1) domain, which was isolated by centrifugation (3). The purified myosin S1 fragment has been determined to be biologically active in an Factin activated ATPase assay (see biological activity assay). Rabbit psoas myosin S1 fragment protein is supplied as a white lyophilized powder.
Figure 1. Diagrammatic representation of the myosin protein and its subfragments
