• Measurement of F-actin-activated myosin ATPase activity
• Biochemical characterization of skeletal myosin II
• Biochemical characterization of myosin II interacting proteins
• Identification of proteins/small molecules that affect myosin II/F-actin interactions

Skeletal myosin II is a motor protein essential for muscle contraction, converting chemical energy from ATP into mechanical force to slide actin filaments. It plays a central role in generating the tension required for voluntary movement, making it critical for locomotion and posture maintenance.

Native myosin II protein is purified from rabbit skeletal muscle. The full-length myosin II heavy chain protein (~200 kDa) is purified with its essential light chains (ELC: ~25 & 17 kDa) and regulatory light chains (RLC: ~20 kDa).

• Formulation: supplied as lyophilized powder
• Composition: when reconstituted to 10 mg/ml, the buffer composition is: 25 mM PIPES pH 7.0, 1.25 M KCl, 1 mM DTT, 2.5% (w/v) sucrose, and 0.5% (w/v) dextran.

Protein purity is assessed by scanning densitometry of Coomassie Blue-stained protein on a4-20% polyacrylamide gel. Purity is determined to be >90% pure.

The biological activity of rabbit myosin II is measured by its rate of F-actin–activated ATP hydrolysis. This is assessed using a standard in vitro F-actin ATPase assay. Quality control requires that, in the presence of F-actin, the ATP hydrolysis rate must be at least 10 times greater than in its absence, and the actin-activated ATPase activity must exceed 300 nmol/min/mg of myosin under the experimental conditions (see datasheet).