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Biochem J 1992 Dec 01;288 ( Pt 2):663-8. doi: 10.1042/bj2880663.
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Monoclonal antibodies for dystrophin analysis. Epitope mapping and improved binding to SDS-treated muscle sections.

Nguyen TM , Ginjaar IB , van Ommen GJ , Morris GE .

A group of 44 monoclonal antibodies (mAbs) raised against the central helical rod (25 mAbs) and C-terminal (19 mAbs) regions of dystrophin were prepared using trpE recombinant fusion proteins as immunogens. Some mAbs cross-react with the structurally related proteins, alpha-actinin and utrophin. Epitope mapping revealed uneven distribution of mAb-binding sites, no mAbs being produced against the C-terminal end of the helical fragment or the cysteine-rich region of the C-terminal dystrophin fragment. The failure of these large regions of the recombinant immunogens to elicit anti-dystrophin antibodies may be because of their inability to fold into the correct dystrophin-like conformation. The mAbs were selected for their ability to recognize 427 kDa dystrophin on Western blots after SDS/PAGE, and/or for immunostaining of the membrane in frozen muscle sections. Although some mAbs obtained by Western-blot screening failed to bind native dystrophin in frozen muscle sections, successful binding could be obtained after SDS or urea treatment of the tissue section to expose the epitopes. This increases the range of mAbs available for detection of dystrophin deletions in muscular dystrophy and evaluation of myoblast therapy.

PubMed ID: 1281410
PMC ID: PMC1132062
Article link: Biochem J

Species referenced: Xenopus
Genes referenced: actn1 dmd.2 utrn
Antibodies: DMD Ab5 Dmd.2 Ab2 Dmd.2 Ab3

References [+] :
Bar, A novel product of the Duchenne muscular dystrophy gene which greatly differs from the known isoforms in its structure and tissue distribution. 1990, Pubmed