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The Structural Conservation of S100 Protein During Evolution: Analysis by Reactivity with a Monoclonal Antibody
Author(s) -
Marks A.,
Law J.,
Mahony J. B.,
Baumal R.
Publication year - 1983
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1983.tb11820.x
Subject(s) - antiserum , polyclonal antibodies , monoclonal antibody , epitope , radioimmunoassay , affinity chromatography , microbiology and biotechnology , s100 protein , antibody , biology , epitope mapping , protein g , chemistry , biochemistry , immunohistochemistry , immunology , enzyme
A hybridoma cell line producing a monoclonal antibody (A4) against bovine S100 protein has been produced by fusing mouse myeloma P3X63/Ag8 cells with spleen cells from a BALB/c mouse immunized with bovine S100 protein. A4 is of the IgG2b subclass and was purified by affinity chromatography on a protein A‐Sepharose column. Brain extracts from several mammalian and one avian species reacted both with polyclonal rabbit anti‐S100 protein antiserum and with A4 in a radio‐immunoassay. Brain extract from dog was a notable exception. It reacted with the rabbit antiserum but not with A4. Therefore A4 reacts with a common epitope that is present on S100 proteins from different vertebrate species but is absent on dog S100 protein.