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M0531

Sigma-Aldrich

Myosin, Calcium activated from porcine heart

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

Synonyme(s) :

Calcium-Activated Myosin, Myosin from Porcine Heart, Porcine Heart Myosin

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About This Item

Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

Source biologique

Porcine heart

Niveau de qualité

Forme

buffered aqueous glycerol solution

Activité spécifique

0.1-0.5 units/mg protein (biuret)

Poids mol.

heavy chain ~200 kDa (each)
light chain 15-20 kDa (each)
~480 kDa

Concentration

≥1.0 mg protein/mL Biuret

Couleur

hazy colorless to light yellow

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Informations sur le gène

Description générale

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).

Actions biochimiques/physiologiques

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 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.
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.

Définition de l'unité

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.

Forme physique

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

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Accuracy of cardiovascular magnetic resonance in myocarditis: comparison of MR and histological findings in an animal model.
Korkusuz H
Journal of Cardiovascular Magnetic Resonance : Official Journal of the Society for Cardiovascular Magnetic Resonance, 12:49 (2010)
K Shioji et al.
FEBS letters, 472(1), 109-113 (2000-04-27)
To examine the possible involvement of a redox regulating mechanism in the pathogenesis of immune-mediated myocarditis, myocarditis was induced by immunization of porcine cardiac myosin in rats and immunohistochemistry and Western blot for thioredoxin (TRX) were performed. Immunohistochemistry for 8-hydroxy-2'-deoxyguanosine
Fc Receptor?Mediated Inhibitory Effect of Immunoglobulin
Therapy on Autoimmune Giant Cell Myocarditis
Concomitant Suppression of the Expression of Dendritic Cells
Shioji K
Circulation Research, 89(6), 540-546 (2001)
Arghavan Jahandideh et al.
Frontiers in medicine, 8, 783596-783596 (2022-01-04)
The 68Gallium-labeled 1,4,7-triazacyclononane-1-glutaric acid-4,7-diacetic acid conjugated radiolabelled arginine-glycine-aspartic acid peptide ([68Ga]Ga-NODAGA-RGD) is a positron emission tomography (PET) tracer binding to cell surface receptor αvβ3 integrin that is upregulated during angiogenesis and inflammation. We studied whether αvβ3 targeting PET imaging can
Lodish H
Molecular Cell Biology (2000)

Articles

Myosins are a family of ATP-dependent motor proteins. Myosin II is the major contractile protein involved in eukaryotic muscle contraction by “walking” along actin microfilaments of the sarcomere

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