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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)

Sinónimos:

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

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10 MG
MXP 3,945.00
50 MG
MXP 14,360.00

MXP 3,945.00


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10 MG
MXP 3,945.00
50 MG
MXP 14,360.00

About This Item

Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.32

MXP 3,945.00


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origen biológico

Porcine heart

Formulario

buffered aqueous glycerol solution

actividad específica

0.1-0.5 units/mg protein (biuret)

mol peso

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

concentración

≥1.0 mg protein/mL Biuret

color

hazy colorless to light yellow

Nº de acceso UniProt

Condiciones de envío

wet ice

temp. de almacenamiento

−20°C

Información sobre el gen

Descripción general

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.[1] Nonmuscle myosins are highly expressed in brain.[2]

Aplicación

Myosin, calcium activated from porcine heart has been used in the induction of experimental autoimmune myocarditis (EAM).[3][4][5]

Acciones bioquímicas o fisiológicas

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 has been shown to be implicated in neurosensory function, vesicle trafficking, determinant partitioning, and cortical function.[6] 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.[1]
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.

Definición de unidad

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.

Forma física

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

Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 2

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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Hyelim Park et al.
Heart rhythm, 15(5), 770-779 (2017-10-01)
Left stellectomy has become an important therapeutic option for patients with potentially fatal arrhythmias. However, the antiarrhythmic mechanism of left stellectomy is not well known. The cholinergic anti-inflammatory pathway (CAIP) is a complex immune mechanism that regulates peripheral inflammatory responses.
Lodish H
Molecular Cell Biology (2000)
Huedayi Korkusuz et al.
Journal of cardiovascular magnetic resonance : official journal of the Society for Cardiovascular Magnetic Resonance, 12, 49-49 (2010-08-28)
Because endomyocardial biopsy has low sensitivity of about 20%, it can be performed near to myocardium that presented as late gadolinium enhancement (LGE) in cardiovascular magnetic resonance (CMR). However the important issue of comparing topography of CMR and histological findings
Siegel GJ
Basic Neurochemistry: Molecular, Cellular and Medical Aspects. (1999)
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

Artículos

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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