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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

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

UniProt accession no.

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

Gene Information

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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


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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 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
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
Vivi F H Jensen et al.
Basic & clinical pharmacology & toxicology, 122(1), 165-175 (2017-08-18)
Peripheral neuropathy is one of the most common complications of diabetic hyperglycaemia. Insulin-induced hypoglycaemia (IIH) might potentially exacerbate or contribute to neuropathy as hypoglycaemia also causes peripheral neuropathy. In rats, IIH induces neuropathy associated with skeletal muscle changes. Aims of
Haruhiko Kondoh et al.
Cardiovascular research, 69(2), 466-475 (2006-01-21)
Cell therapy is a promising strategy for ischemic cardiomyopathy. However, the direct injection method has limitations for generalized cell delivery, especially in dilated cardiomyopathy (DCM). We hypothesized that a sheet-shaped myoblast graft would be superior to direct injection for improving

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