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A new monoclonal antibody recognizing the amino‐terminal consensus sequence of vertebrate intermediate filament proteins
Author(s) -
Escurat Michel,
Phamgia Hai,
Huc Claude,
Pouplard-Barthelaix Annick,
Boitard Christian,
Bach Jean-François,
Gros François,
Portier Marie-Madeleine
Publication year - 1989
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(89)80950-0
Subject(s) - epitope , intermediate filament , peripherin , monoclonal antibody , biology , vimentin , peptide sequence , microbiology and biotechnology , neurofilament , intermediate filament protein , antibody , desmin , amino acid , epitope mapping , biochemistry , genetics , cytoskeleton , gene , immunohistochemistry , immunology , cell
The mouse monoclonal antibody ME 101 raised against human peripherin, an intermediate filament protein (IFP) specific to well defined neuronal populations, recognizes all the major classes of vertebrate IFP in immunoblotting assays. Desmin, GFAP, vimentin, peripherin and the lightest neurofilament protein (NF‐L) were cleaved into carboxy‐ and amino‐terminal halves by N ‐chlorosuccinimide at their unique trytophan residue. Whereas the antibody directed against the epitope common to every IFP (intermediate filament antigen or IFA) and located on the carboxy‐terminal end of the rod domain recognizes the carboxy‐terminal half, the ME 101 antibody, as the present study illustrates, recognizes specifically the amino‐terminal half. From the amino acid sequence data of IFP, it is deduced that the cognate epitope is localized on the amino‐terminal part of coil la.