Skip to Content
Merck
All Photos(2)

Documents

SAB4200764

Sigma-Aldrich

Anti-Dystrophin antibody, Mouse monoclonal

enhanced validation

clone MANDYS8, purified from hybridoma cell culture

Synonym(s):

Anti-DMD

Sign Into View Organizational & Contract Pricing


About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

MANDYS8, monoclonal

form

buffered aqueous solution

mol wt

~427 kDa

species reactivity

porcine, rabbit, mouse, rat, human

enhanced validation

independent
Learn more about Antibody Enhanced Validation

concentration

~1.0 mg/mL

technique(s)

immunoblotting: suitable
immunohistochemistry: 5-10 μg/mL using acetone fixed rat tongue frozen sections

isotype

IgG2b

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DMD(1756)

General description

Anti-Dystrophin antibody, Mouse monoclonal (mouse IgG2b isotype) is derived from the MANDYS8 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from mouse immunized with fragment of recombinant human dystrophin. Dystrophin is a 427 kD protein which joins the actin cytoskeleton to laminin. It possesses multiple domains and is localized to the extracellular matrix. Dystrophin contains NH2-terminal domain for actin binding. The C-terminal domain interacts with dystrophin associated protein (DAP).
Dystrophin is a rod-shaped cytoskeletal protein located to the periphery (plasma membrane) of normal striated muscle fibers.

Specificity

Anti-Dystrophin antibody, Mouse monoclonal specifically recognizes an epitope located on the rod domain of the human dystrophin molecule.

Immunogen

recombinant human dystrophin

Application

Anti-Dystrophin antibody, Mouse monoclonal has been used in immunoblotting and immunohistochemistry.

Biochem/physiol Actions

Dystrophin is known to prevent muscle fibre injury due to contraction.

Physical form

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

Other Notes

This product is for R&D use only, not for drug, household, or other uses.

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Anna Cho et al.
Muscle & nerve, 55(5), 727-734 (2016-09-07)
Duchenne and Becker muscular dystrophies (DMD and BMD) are allelic X-linked recessive muscle diseases caused by mutations in the large and complex dystrophin gene. We analyzed the dystrophin gene in 507 Korean DMD/BMD patients by multiple ligation-dependent probe amplification and
Assembly of the dystrophin-associated protein complex does not require the dystrophin COOH-terminal domain
Crawford GF, et al.
The Journal of Cell Biology, 150(6), 1399-1410 (2000)
Applications of CRISPR technologies in research and beyond
Barrangou R and Doudna JA
Nature Biotechnology, 34(9), 933-933 (2016)
Immunofluorescence microscopy of SNAP23 in human skeletal muscle reveals colocalization with plasma membrane, lipid droplets, and mitochondria
Strauss JA, et al.
Physiological Reports, 4(1), e12662-e12662 (2016)
Juliette A Strauss et al.
Physiological reports, 4(1) (2016-01-07)
Synaptosomal-associated protein 23 (SNAP23) is a SNARE protein expressed abundantly in human skeletal muscle. Its established role is to mediate insulin-stimulated docking and fusion of glucose transporter 4 (GLUT4) with the plasma membrane. Recent in vitro research has proposed that SNAP23

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service