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D8043

Sigma-Aldrich

Monoclonal Anti-Dystrophin antibody produced in mouse

clone MANDRA1, ascites fluid

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About This Item

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

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

MANDRA1, monoclonal

contains

15 mM sodium azide

species reactivity

rat, human, mouse, fish

technique(s)

indirect immunofluorescence: 1:100 using freshly dissected and frozen human or animal muscle tissue.
microarray: suitable

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DMD(1756)
mouse ... Dmd(13405)
rat ... Dmd(24907)

General description

Dystrophin is a muscle membrane protein (427 kDa) which is absent, reduced or altered as a result of mutation in Duchenne and Becker muscular dystrophies (DMD/BMD) or its homologue in the mouse. Severe DMD is associated with a marked dystrophin deficiency whereas patients with the milder form of DMD show less pronounced abnormalities of protein expression. Because abnormalities in the protein expression occur specifically in patients with these types of muscular dystrophy, dystrophin analysis may be used to distinguish these conditions from other neuromuscular diseases. Predictions from the sequence suggest a structural protein on the inner face of the membrane, consisting of a 25-repeat, rod-like triple-helical domain separating an N-terminal actin-binding domain from two C-terminal domains, one of which is rich in cysteine. The large size of dystrophin and its low abundance (<0.01% of the total muscle protein) are a hindrance to the isolation of intact, native protein for structure/function studies.
The antibody recognizes an epitope located on the 128 amino acids at the end of the C-terminal domain of the human dystrophin molecule (amino acid residues 3558-3684). Immunohistochemical staining of muscle tissue results in a clear labeling confined to the periphery (plasma membrane) of normal striated muscle fibers. By immunoblotting, the antibody stains dystrophin (427 kDa) in muscle and brain extracts. It also stains the 70-75 kDa protein known as Apo-Dystrophin-1 or Dp71.4 This is detected in the brain as well as in lymphoblastoid cells, cultures of brain astroglial and neuronal cells, liver and Hep G2 cells (human hepatoma). The epitope recognized by the antibody is sensitive to formalin fixation and paraffin embedding. The antibody exhibits a wide interspecies cross-reactivity. It is useful in ELISA and capture ELISA. The antibody is specific to dystrophin and does not react with α-actinin and utrophin, an autosomal homologue of dystrophin, also called dystrophin-related protein (DRP).

Specificity

The antibody recognizes an epitope located on the 128 amino acids at the end of the C-terminal domain of the human dystrophin molecule (amino acid residues 3558-3684). Immunohistochemical staining of muscle tissue results in a clear labeling confined to the periphery (plasma membrane) of normal striated muscle fibers. By immunoblotting, the antibody stains dystrophin (427 kDa) in muscle and brain extracts. It also stains the 70-75 kDa protein known as Apo-Dystrophin-1 or Dp71.4 This is detected in the brain as well as in lymphoblastoid cells, cultures of brain astroglial and neuronal cells, liver and Hep G2 cells (human hepatoma). The epitope recognized by the antibody is sensitive to formalin fixation and paraffin embedding. The antibody exhibits a wide interspecies cross-reactivity. It is useful in ELISA and capture ELISA. The antibody is specific to dystrophin and does not react with α-actinin and utrophin, an autosomal homologue of dystrophin, also called dystrophin-related protein (DRP).

Immunogen

fusion protein containing the C-terminal amino acids of human dystrophine.

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)
Western Blotting (1 paper)
Mouse monoclonal clone MANDRA1 anti-Dystrophin antibody may be used for the localization of dystrophin using various immunochemical assays such as ELISA, capture ELISA, immunoblot, and immunohistochemistry. Monoclonal antibodies against defined regions of dystrophin provide a means for studying its structure and function, interactions with other proteins and the nature of the partial gene products produced in some patients carrying deletions in the dystrophin gene. The antibodies are useful in the prenatal or post-abortion diagnosis of muscular dystrophy carriers by immunohistological analyses.

Target description

The C-terminal domain of the human dystrophin molecule (amino acids residues 3558-3684) is present in normal muscle tissue. It is also present in nearly all Becker muscular dystrophies, but is absent in cases of Duchenne muscular dystrophies and in the dystrophic mouse (mdx).

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

13 - Non Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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G E Morris et al.
Journal of immunological methods, 161(1), 23-28 (1993-05-05)
A novel approach to the quantitation of the muscular dystrophy protein, dystrophin, in muscle extracts is described. The two-site ELISA uses two monoclonal antibodies against dystrophin epitopes which lie close together in the rod domain of the dystrophin molecule in
Kazumi Zushi et al.
Journal of the Japanese Physical Therapy Association = Rigaku ryoho, 15(1), 1-8 (2012-01-01)
The purpose of this study was to investigate the effect of reloading on atrophied muscle and the time course of hypertrophy and regeneration. Forty-nine male Wistar rats were randomly assigned to groups for hindlimb suspension (HS), hindlimb suspension and reloading
Julia Saifetiarova et al.
Journal of neuroscience research, 95(7), 1373-1390 (2017-04-04)
Bidirectional interactions between neurons and myelinating glial cells result in formation of axonal domains along myelinated fibers. Loss of axonal domains leads to detrimental consequences on nerve structure and function, resulting in reduced conductive properties and the diminished ability to
Beatrice Nico et al.
Laboratory investigation; a journal of technical methods and pathology, 90(11), 1645-1660 (2010-08-18)
In this study, we investigated the involvement of dystrophin-associated proteins (DAPs) and their relationship with the perivascular basement membrane in the brains of mdx mice and controls at the age of 2 months. We analyzed (1) the expression of glial
Jérome Fleuriet et al.
Scientific reports, 10(1), 11927-11927 (2020-07-19)
The ability of sustained treatment of a single extraocular muscle with glial cell line-derived neurotrophic factor (GDNF) to produce a strabismus in infant non-human primates was tested. Six infant non-human primates received a pellet containing GDNF, releasing 2 µg/day for

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