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Monoclonal antibodies against chordin Use in structural and immunohistochemical studies
Author(s) -
Preobrazhensky A.A.,
Rodionova A.I.,
Trakht I.N.,
Rukosuev V.S.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80415-5
Subject(s) - chordin , epitope , monoclonal antibody , immunohistochemistry , microbiology and biotechnology , chemistry , antibody , biology , embryo , immunology , gastrulation , embryogenesis
Eight MAbs have been developed against chordin and designated as At2–At9. It is shown that all antibodies are directed against identical, spatially overlapping or closely positioned epitopes of chordin. The chordin molecule has repetitive sites wherein epitopes for the eight MAbs are located. This site lies within a protein ase‐resistant fragment of chordin, presumably a glycopeptide, of molecular mass between 2 and 10 kDa. Fluorescence staining of cryostat sections from stellate sturgeon with the use of At5 (indirect Coons' method) has revealed a positive reaction with notochord cells and sheath and with the spinal cord. No significant reaction with cartilage, muscle and kidney was detected.