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Generation and Characterization of Rat Monoclonal Antibodies Against Human Serum Amyloid A
Author(s) -
YAMADA T,
HIRANO N,
KURODA T,
OKUDA Y,
ITOH Y
Publication year - 1997
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1046/j.1365-3083.1997.d01-108.x
Subject(s) - monoclonal antibody , serum amyloid a , antibody , recombinant dna , amyloidosis , amyloid (mycology) , immunohistochemistry , chemistry , residue (chemistry) , microbiology and biotechnology , epitope , biology , biochemistry , immunology , medicine , pathology , inorganic chemistry , inflammation , gene
Monoclonal antibodies against human serum amyloid A (SAA) were generated in rat (which seems not to have mature SAA proteins) by immunizing intact human SAA. Thirteen clones selected by initial screening were analysed based on reactivity with synthetic peptides of SAA and with carboxyl‐terminal truncated recombinant SAA. Antibodies were divided into four types, i.e. those recognizing the area around residue 18, 30, 90, and 100, respectively, of SAA. The antibody to the carboxyl terminus (around residue 100) of SAA, when subjected to immunohistochemistry for amyloid deposits in specimens from patients with reactive amyloidosis, always yielded negative reactivity, supporting the general concept that the carboxyl terminus of SAA is absent from human AA deposits.