Myosin II protein: rabbit skeletal muscle

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.

	Figure 1. Diagrammatic representation of the myosin II protein and its subfragments. Myosin II or conventional myosin is a hexameric protein consisting of two heavy chains and two light chains. Myosin II can be proteolytically cleaved into heavy meromyosin (HMM, Cat.# MH01) and light meromyosin (LMM) by α-chymotrypsin. Heavy meromyosin consists of the myosin head subfragment-1 domain (S1), its associated light chains (essential light chains and regulatory light chains), and the coiled-coil subfragment -2 domain. Light meromyosin consists of coiledcoil protein structure. The myosin S1-subfragment is produced by papain digestion of HMM.

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 (see Figure 2).

	Figure 2. Myosin II protein purity determination. A 20 µg sample of MY02 was separated by electrophoresis in a 4-20% SDS-PAGE system, and stained with Coomassie Blue. Arrow indicates the myosin heavy chain (approx. 200 kDa), arrowheads indicate the RLC (approx. 20 kDa) and two ELC isoforms (approx. 25 and 17 kDa). Protein quantitation was performed using the Precision Red Protein Assay Reagent (Cat.# ADV02).

For product Datasheets and MSDSs please click on the PDF links below.   For additional information, click on the FAQs tab above or contact our Technical Support department at tservice@cytoskeleton.com

Product Description

MSDS

Datasheet

Cat #

Myosin II protein: rabbit skeletal muscle MY02

Harris, E. S., Li, F. and Higgs, H. N. (2004). The mouse formin, FRLα, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments. J. Biol. Chem. 279, 20076-20087.

Gallo, G., Yee, H. F., Jr. and Letourneau, P. C. (2002). Actin turnover is required to prevent axon retraction driven by endogenous actomyosin contractility. J. Cell Biol. 158, 1219-1228.

Coming soon!   If you have any questions concerning this product, please contact our Technical Service department at tservice@cytoskeleton.com