Product Uses Include

• Measurement of F-actin activated ATPase activity

• Identification/characterization of proteins or small molecules that affect heavy meromyosin
  ATPase activity

• Identification/characterization of proteins or small molecules that affect heavy meromyosin Factin
  interaction

Material
Heavy meromyosin has been produced by α-chymotrypsin proteolytic cleavage of full-length myosin II protein isolated from rabbit skeletal muscle. Heavy meromyosin consists of an active motor fragment consisting of two head domains connected by their subfragment-2 (S2) regions and two pairs of light chains, essential light chain (ELC) and regulatory light chain (RLC), see Figure 1. Heavy meromyosin has been determined to be biologically active in an F-actin activated ATPase assay. Heavy meromyosin is supplied as a white lyophilized powder. When reconstituted in nanopure water, the protein will be in the following buffer: 10 mM Imidizole pH 7.0, 50 mM KCl, 3 mM MgCl2, 1 mM DTT, 5% sucrose and 1% dextran. The lyophilized protein is stable at 4°C desiccated (<10% humidity) for 1 year.