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Myosin Cardiac Muscle

Myosin Cardiac Muscle

Item no.	MY03-B
Manufacturer	Cytoskeleton
Amount	20 x 1 mg
Quantity options	5 x 1 mg 20 x 1 mg
Category	Neuroscience Neural Lineage Markers Peptides & Proteins Recombinant Proteins Cell Biology Cell Status Necrosis Cytoskeleton Motor proteins Microfilaments
Type	Proteins
Specific against	other
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).
Citations	Coming soon! For the most recent publications citing this product, please contact our Technical Service department at infohoelzel.de
ECLASS 10.1	32160409
ECLASS 11.0	32160409
UNSPSC	12352202
Alias	Actin, Actin Protein, Cardiac myosin protein, cardiac myosin, F-actin activated ATP hydrolysis
Similar products	Actin, Actin Protein, Cardiac myosin protein, cardiac myosin, F-actin activated ATP hydrolysis
Shipping condition	Room temperature
Available
Shipping Temperature	AT
Storage Conditions	On Arrival: 4°C
Delivery Time	1-2 Weeks
FAQs	Question 1: Does this myosin contain both light and heavy chains and all other subunits? Answer 1: Yes, this protein is full length myosin motor protein isolated from bovine cardiac muscle. The myosin protein contains the two heavy chains and two light chains, the essential light chain (ELC) and regulatory light chain (RLC). Question 2: Does this myosin have ATPase activity that is activated by actin filaments? Answer 2: Yes, the biological activity test for the myosin protein is in vitro measurement of myosin&rsquo, s ATPase activity in the activating presence of actin filaments. Stringent quality control ensures that in the presence of F-actin, bovine cardiac myosin will have a minimum hydrolysis rate 2 fold greater than in the absence of F-actin. This myosin has approximately 20 times less ATPase activity than skeletal muscle myosin.
Weight (grams)	60
Product Uses	Drug discovery target in cardiac research 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	Cardiac myosin protein has been purified from bovine heart muscle. The full length myosin protein has been purified with its essential light chains (ELC) and regulatory light chains (RLC), see Figure 1 and 2. Cardiac myosin has been determined to be biologically active in an F-actin activated ATPase assay, but it is not recommended for use in motility assays because of auto-inhibition (Protease digests with alpha-chymotrypsin and papain may create a subfragment that has F-actin moving properties. Cardiac myosin 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 4C desiccated (< 10% humidity) for 1 year.
Biological Activity	The biological activity of cardiac myosin 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. Rabbit myosin (Cat.# MY02) is also available for comparison studies.
Figure 1 Legend	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 ?-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.

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

MY03-B.pdf

MY03-B-datasheet.pdf

MY03-B-safety-datasheet.pdf