M0531

Myosin, Calcium activated from porcine heart

buffered aqueous glycerol solution, 0.1-0.5 units/mg protein (biuret)

• Synonym(e): Calcium-Activated Myosin, Myosin from Porcine Heart, Porcine Heart Myosin
• UNSPSC Code: 12352202
• NACRES: NA.32
• MDL number: MFCD00131645
• Form: buffered aqueous glycerol solution
• Biological source: Porcine heart
• Mol wt: heavy chain ~200 kDa (each), light chain 15-20 kDa (each), ~480 kDa

Eigenschaften

• biological source: Porcine heart
• form: buffered aqueous glycerol solution
• specific activity: 0.1-0.5 units/mg protein (biuret)
• mol wt: heavy chain ~200 kDa (each), light chain 15-20 kDa (each), ~480 kDa
• concentration: ≥1.0 mg protein/mL Biuret
• color: hazy colorless to light yellow
• UniProt accession no.: A0A5G2QTZ6
• shipped in: wet ice
• storage temp.: −20°C
• Gene Information: pig ... MYHC(396711)

Beschreibung

General description

Myosin is one of three classes of cytoskeletal motor proteins that have been identified. The others are kinesins and dyneins. Myosin family members contain globular head domain with actin and ATP binding site, α-helical neck region and a coiled–coiled tail domain. Nonmuscle myosins are highly expressed in brain.

Application

Myosin, calcium activated from porcine heart has been used in the induction of experimental autoimmune myocarditis (EAM).

Biochem/physiol Actions

Myosin has been shown to be implicated in neurosensory function, vesicle trafficking, determinant partitioning, and cortical function. Myosins with actin-stimulated ATPase activity play a vital role in various cellular movements. Myosins I and V mediates vesicle translocation. Myosin II with a long rod like tail domain, assembles into a bipolar thick filament and facilitate muscle contraction.

Interacts with actin in muscle and non-muscle cells; involved in neurosensory function, vesicle trafficking, determinant partitioning, and cortical function.

Myosin interacts with actin in muscle and non-muscle cells. Myosin molecules consist of two major regions: tails (rods) and heads. They aggregate into filaments through the tail region and interact with actin and with ATP through the head region. Myosin molecules spontaneously assemble into filaments in solutions of physiologic ionic strength and pH. Thick filament consists mainly of myosin molecules. Myosin is activated by the enzyme ATPase. This activation is the immediate source of the free energy that drives muscle contraction. It binds to the polymerized form of actin, the major constituent of the thin filament. Multiple forms of myosin heavy chains exist for each muscle type-skeletal, cardiac, smooth and non-muscle. Isomyosin forms exist in different types of skeletal muscle, depending on the physiological function of the muscle. These are designated as type I (slow-twitch) and type II (fast-twitch). Myosin is one of three classes of cytoskeletal motor proteins that have been identified. The others are kinesins and dyneins. These three types of proteins are thought to be responsible for the many movements that occur in cells. Myosin has been shown to be involved in neurosensory function, vesicle trafficking, determinant partitioning, and cortical function.

Myosin interacts with actin in muscle and non-muscle cells. Myosin is one of three classes of cytoskeletal motor proteins that have been identified. The others are kinesins and dyneins. These three types of proteins are thought to be responsible for the many movements that occur in cells. Myosin has been shown to be involved in neurosensory function, vesicle trafficking, determinant partitioning, and cortical function.

Physical form

Solution in 50% glycerol containing 0.6 M KCl and 10 mM potassium phosphate buffer, pH 6.8.

Other Notes

One unit will liberate 1.0 μmole of inorganic phosphorus from ATP per min at pH 9.0 at 25 °C in the presence of calcium.

Sicherheitshinweise

• Lagerklasse: 10 - Combustible liquids
• wgk: WGK 2
• flash_point_f: Not applicable
• flash_point_c: Not applicable