Active Native Rabbit Heavy Meromyosin Protein

• Cat.No.: MYS-01R
• Product Overview: Heavy meromyosin has been produced by α-chymotrypsin proteolytic cleavage of full-length myosin II protein isolated from rabbit skeletal muscle. Heavy meromyosin has been determined to be biologically active in an F-actin activated ATPase assay.

Specification

• Species: Rabbit
• Source: Skeletal muscle
• Description: 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).
• Form: White lyophilized powder
• Bio-activity: The biological activity of rabbit heavy meromyosin is determined from its rate of F-actin activated ATP hydrolysis. A standard biological assay for monitoring ATP hydrolysis by heavy meromyosin consists of an in vitro F-actin ATPase assay. Stringent quality control ensures that in the presence of F-actin, rabbit heavy meromyosin will have a minimum hydrolysis rate 500 fold greater than in the absence of F-actin.
• Purity: Protein purity is determined by scanning densitometry of Coomassie Blue stained protein on a 4-20% gradient polyacrylamide gel. Heavy meromyosin protein was determined to be 70% pure
• Applications: 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
• Stability: The lyophilized protein is stable at 4 centigrade desiccated (<10% humidity) for 1 year.
• Storage: Upon arrival store at 4 centigrade (desiccated)
• Storage Buffer: 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.
• Reconstitution: Briefly centrifuge to collect the product at the bottom of the tube. The protein should be reconstituted to 5 mg/ml by the addition of 10 µl of Milli-Q 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% (w/ v) sucrose and 1% (w/v) dextran. In order to maintain high biological activity of the protein, it is recommended that the protein solution be aliquoted into "experiment sized" amounts, snap frozen in liquid nitrogen and stored at -70 centigrade. The protein is stable for 6 months if stored at -70 centigrade. The protein should not be ex- posed to repeated freeze-thaw cycles. The lyophilized protein is stable at 4 centigrade desiccated (<10% humidity) for 1 year.