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Myosin II protein - rabbit skeletal muscle

Myosin II protein - rabbit skeletal muscle (MY02-GRP)

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Description

Product Uses Include

  • Measurement of F-actin activated myosin ATPase activity
  • Identification/characterization of proteins or small molecules that affect myosin II ATPase activity
  • Identification/characterization of proteins or small molecules that affect the myosin II - F-actin interaction
  • Control myosin ATPase activity in drug discovery screening projects

Material
Myosin II protein has been purified from rabbit skeletal muscle. The full length myosin II protein has been purified with its essential light chains (ELC) and regulatory light chains (RLC), see Figure 1 and 2. Myosin II has been determined to be biologically active in an F-actin activated ATPase assay. Rabbit skeletal muscle myosin II is not recommended for use in motility assays. Rabbit myosin II protein is supplied as a white lyophilized powder. When reconstituted in nanopure water, the protein will be in the following buffer: 100 mM Imidizole pH 7.5, 2.4 M KCl, 0.2 mM DTT, 5% sucrose and 1% dextran. The lyophilized protein is stable at 4°C desiccated (<10% humidity) for 1 year. 

Purity
Protein purity is determined by scanning densitometry of Coomassie Blue stained protein on a 4-20% gradient polyacrylamide gel. Myosin protein is 95% pure.

Biological Activity
The biological activity of rabbit myosin II is determined from its rate of F-actin activated ATP hydrolysis. A standard biological assay for monitoring ATP hydrolysis by myosin consists of an in vitro F-actin ATPase assay (Cat. # BK054). Stringent quality control ensures that in the presence of F-actin, rabbit myosin will have a minimum hydrolysis rate 10 fold greater than in the absence of F-actin, which is comparable to published results.

Specifications

Storage 4°C