Product Uses
Measurement of calcium activated cardiac HMM ATPase activity when bound to thin filaments.
Identification/characterization of proteins or small molecules that affect the TT complex regulation and cardiac HMM ATPase activity
Identification/characterization of proteins or small molecules that affect cardiac HMM / F- actin interaction
Materials
Cardiac myosin protein has been purified from bovine heart tissue (1,2,3). 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 a-chymotrypsin in the presence of MgCl2 to liberate the soluble heavy fragment (HMM) domain, which was isolated by centrifugation followed by anionic exchange chromatography to remove S1 (2,3). The purified myosin HMM fragment has been determined to be biologically active in an F-actin activated ATPase assay (see biological activity assay). Bovine cardiac myosin S1 fragment protein is supplied as a white lyophilized powder.
Figure 1. Diagrammatic representation of the myosin protein and its subfragments