• In vitro assays that may benefit from using a cardiac-muscle source of actin
• In vitro characterization of actin-binding proteins (ABPs)
• In vitro study of actin dynamics

Cardiac actin has been purified from bovine heart muscle and is composed of 84% α-cardiac and 16% α-skeletal actin isoforms. Cardiac actin has
an approximate molecular weight of 43 kDa and is supplied as a white lyophilized powder.

Protein purity is assessed using scanning densitometry of Coomassie-stained SDS-PAGE gels. AD99 is >99% pure.

The biological activity of cardiac actin is assessed by its ability to efficiently polymerize into filaments in vitro, which can be separated from unpolymerized components using a spin-down assay. Rigorous quality control ensures that >90% of the muscle actin polymerizes under these conditions.