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M1570

Sigma-Aldrich

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

enhanced validation

clone MY-32, purified from hybridoma cell culture

Synonyma:

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

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About This Item

MDL number:
MFCD00145920
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

200

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

MY-32, monoclonal

form

buffered aqueous solution

species reactivity

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

packaging

antibody small pack of 25 μL

enhanced validation

independent
Learn more about Antibody Enhanced Validation

concentration

~1.0 mg/mL

technique(s)

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

isotype

IgG1

UniProt accession no.

P12882

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... MYH1(4619) , MYH2(4620)
mouse ... Myh1(17879) , Myh2(17882)
rat ... Myh1(287408) , Myh2(691644)

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General description

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.

Immunogen

rabbit muscle myosin.

Application

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.

Physical form

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

Disclaimer

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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Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

Osvědčení o analýze (COA)

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Navštívit knihovnu dokumentů

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.
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
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
David W Hammers et al.
EMBO molecular medicine, 9(4), 531-544 (2017-03-09)
Growth and differentiation factor (GDF) 11 is a member of the transforming growth factor β superfamily recently identified as a potential therapeutic for age-related cardiac and skeletal muscle decrements, despite high homology to myostatin (Mstn), a potent negative regulator of
Miyuki Sakuma et al.
The European journal of neuroscience, 43(3), 451-462 (2015-09-04)
Motor axons in peripheral nerves have the capacity to regenerate after injury. However, full functional motor recovery rarely occurs clinically, and this depends on the nature and location of the injury. Recent preclinical findings suggest that there may be a
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