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M1570

Sigma-Aldrich

Anti-Myosin (Skeletal, Fast) antibody, Mouse monoclonal

enhanced validation

clone MY-32, purified from hybridoma cell culture

Sinonimo/i:

Monoclonal Anti-Myosin (Skeletal, Fast) antibody produced in mouse

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

mouse

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

purified immunoglobulin

Tipo di anticorpo

primary antibodies

Clone

MY-32, monoclonal

Forma fisica

buffered aqueous solution

Reattività contro le specie

rat, chicken, rabbit, mouse, human, bovine, guinea pig, feline

Confezionamento

antibody small pack of 25 μL

Convalida avanzata

independent
Learn more about Antibody Enhanced Validation

Concentrazione

~1.0 mg/mL

tecniche

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 10-20 μg/mL using porcine tongue
microarray: suitable
western blot: 0.5-1.0 μg/mL using total extract of rabbit skeletal muscle

Isotipo

IgG1

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

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Descrizione generale

Localizes an epitope on the myosin heavy chain. Stains the fast (type II) and neonatal isomyosin molecules found in skeletal muscle, but does not stain cardiac muscle, smooth muscle or non-muscle myosin in cultured cells. Does react with human rhabdomyosarcomas.

Immunogeno

rabbit muscle myosin.

Applicazioni

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)
The level of mysosin (fast) in serum samples from sportsmen with past injury was determined by western blot using monoclonal mouse anti-myosin (skeletal/fast) as the primary antibody at a dilution of 1:90000.

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Esclusione di responsabilità

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1


Certificati d'analisi (COA)

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Charlotte Capitanchik et al.
Nucleus (Austin, Tex.), 9(1), 410-430 (2018-06-19)
Laminopathies yield tissue-specific pathologies, yet arise from mutation of ubiquitously-expressed genes. A little investigated hypothesis to explain this is that the mutated proteins or their partners have tissue-specific splice variants. To test this, we analyzed RNA-Seq datasets, finding novel isoforms
Yanlin Wang et al.
Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology, 40(6), 1255-1265 (2019-03-21)
Myotonic dystrophy type 1 (DM1) is caused by CTG nucleotide repeat expansions in the 3'-untranslated region (3'-UTR) of the dystrophia myotonica protein kinase (DMPK) gene. The expanded CTG repeats encode toxic CUG RNAs that cause disease, largely through RNA gain-of-function.
Tomohiko Akiyama et al.
Scientific reports, 8(1), 1189-1189 (2018-01-21)
Direct generation of skeletal muscle cells from human pluripotent stem cells (hPSCs) would be beneficial for drug testing, drug discovery, and disease modelling in vitro. Here we show a rapid and robust method to induce myogenic differentiation of hPSCs by
Maegen A Ackermann et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 27(8), 3217-3228 (2013-05-10)
Myosin binding protein C (MyBP-C) is expressed in striated muscles, where it plays key roles in the modulation of actomyosin cross-bridges. Slow MyBP-C (sMyBP-C) consists of multiple variants sharing common domains but also containing unique segments within the NH2 and
Jin Young Lee et al.
Frontiers in cell and developmental biology, 8, 565826-565826 (2020-11-27)
Skeletal muscle and bone are highly interrelated, and previous proteomic analyses suggest that lumican is one of muscle-derived factors. To further understand the role of lumican as a myokine affecting adjacent bone metabolism, we investigated the effects of lumican on

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