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Merck

A4335

Sigma-Aldrich

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

clone MY-32, purified from hybridoma cell culture

Synonym(s):

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

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About This Item

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

Pricing and availability is not currently available.

biological source

mouse

Quality Level

conjugate

alkaline phosphatase conjugate

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

MY-32, monoclonal

form

buffered aqueous glycerol solution

species reactivity

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

technique(s)

direct immunofluorescence: 1:150 using formalin-fixed, paraffin-embedded human or animal skeletal muscle sections

isotype

IgG1

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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.
Monoclonal Anti-Myosin (Skeletal, Fast) (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse.

Specificity

Monoclonal Anti-Myosin (Skeletal, Fast) specifically binds to an epitope in adult rat skeletal myosin heavy chains IIa, IIb and IId (IIx) (in fast-twitch fibers)†. The antibody product is also reactive in humans, bovines, cats, rabbits, mice, guinea pigs and chickens.

Immunogen

rabbit muscle myosin.

Application

Monoclonal Anti-Myosin (Skeletal, Fast) Alkaline Phosphatase antibody produced in mouse has been used for the detection and localization of skeletal muscle fast and neonatal myosins using immunohistochemistry. It may be used in muscle fiber typing, in studies of in vivo and in vitro muscle development and in the diagnosis of rhabdomyosarcomas.
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.

Biochem/physiol Actions

Myosin (Skeletal, Fast) is useful not only in fiber typing but also in detection of myogenic tumors. It enables retrospective as well as prospective fiber typing using formalin-fixed, paraffin-embedded material.
Myosins are motor proteins that interact with actin filaments to regulate cell movement. Myosins also modulate cell shape and signaling. Skeletal muscle myosins have three ′fast′ myosin heavy chains isoforms (IIa, IIx, and IIb), a ′slow′ beta-myosin heavy chain isoform and three major myosin light-chain (MLC) isoforms. These myosin isoforms regulate skeletal muscle shortening.

Physical form

Solution in 0.05 M Tris buffer, pH 8.0, containing 1% bovine serum albumin, 1 mM MgCl2, 50% glycerol, and 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 Code

10 - Combustible liquids

WGK

WGK 2


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S Schiaffino et al.
Journal of applied physiology (Bethesda, Md. : 1985), 77(2), 493-501 (1994-08-01)
Skeletal muscles of different mammalian species contain four major myosin heavy-chain (MHC) isoforms: the "slow" or beta-MHC and the three "fast" IIa-, IIx-, and IIb-MHCs; and three major myosin light-chain (MLC) isoforms, the "slow" MLC1s and the two "fast" MLC1f
Charles A Stuart et al.
Journal of strength and conditioning research, 31(3), 798-808 (2016-07-06)
Stuart, CA, Lee, ML, South, MA, Howell, MEA, Cartwright, BM, Ramsey, MW, and Stone, MH. Pre-training muscle characteristics of subjects who are obese determine how well exercise training will improve their insulin responsiveness. J Strength Cond Res 31(3): 798-808, 2017-Only
Charles A Stuart et al.
Journal of applied physiology (Bethesda, Md. : 1985), 123(4), 894-901 (2017-07-01)
Resistance training of healthy young men typically results in muscle hypertrophy and a shift in vastus lateralis composition away from type IIx fibers to an increase in IIa fiber content. Our previous studies of 8 wk of resistance training found
Glenda Comai et al.
Developmental cell, 31(5), 654-667 (2014-12-10)
The myogenic regulatory genes Myf5, Mrf4, Myod, and Myogenin likely arose by gene duplications during evolution, presumably to address the more demanding requirements of the vertebrate body plan. Two cell lineages were proposed to be regulated independently by Myf5 and
Katy C Liu et al.
Bioarchitecture, 2(5), 158-170 (2012-09-08)
The development of cell-cell junctions was a fundamental step in metazoan evolution, and human health depends on the formation and function of cell junctions. Although it has long been known that actin and conventional myosin have important roles in cell

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