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Merck

M0531

Myosin, Calcium activated from porcine heart

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

Synonim(y):

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

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Informacje o tej pozycji

UNSPSC Code:
12352202
NACRES:
NA.32
MDL number:
Form:
buffered aqueous glycerol solution
Biological source:
Porcine heart
Mol wt:
heavy chain ~200 kDa (each), light chain 15-20 kDa (each), ~480 kDa
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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.

shipped in

wet ice

storage temp.

−20°C

Quality Level

Gene Information

pig ... MYHC(396711)

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

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. 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.

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.
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Klasa składowania

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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)
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)
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
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.

Produkty

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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