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Development of a monoclonal antibody against recombinant neuroendocrine 7B2 protein
Author(s) -
van Duijnhoven Hans L.P.,
Ayoubi Torik A.Y.,
Timmera Erika D.J.,
Braks Anneke A.M.,
Roebroek Anton J.M.,
Martens Gerard J.M.,
van de Ven Wim J.M.
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)81125-1
Subject(s) - immunoprecipitation , western blot , monoclonal antibody , microbiology and biotechnology , recombinant dna , immunohistochemistry , xenopus , blot , biology , antibody , chemistry , biochemistry , gene , immunology
Mouse monoclonal antibody MON‐100 was raised against the neuroendocrine protein 7B2 using bacterially produced hybrid proteins. In Western blot analysis, MON‐100 reacted with 3 different 7B2 hybrid proteins and not with the respective carrier proteins. Furthermore, MON‐100 was reactive with recombinant 7B2 cleaved from a hybrid protein. In an immunohistochemical study, MON‐100 exhibited strong reactivity with the intermediate lobe of the Xenopus pituitary gland, a tissue previously shown to contain 7B2 mRNA. Using MON‐100, immunoprecipitation analysis of newly synthesized proteins produced by in vitro incubated Xenopus neurointermediate lobes revealed the biosynthesis of a single protein of M r 24 kDa, the expected size of the 7B2 protein. It appears, therefore, that the anti‐7B2 monoclonal antibody MON‐100 can be successfully used for Western blot analysis and immunohistochemical analysis as well as for immunoprecipitation experiments.