Literature DB >> 9583998

Generation and characterization of rat monoclonal antibodies against human serum amyloid A.

T Yamada1, N Hirano, T Kuroda, Y Okuda, Y Itoh.   

Abstract

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.

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Year:  1997        PMID: 9583998     DOI: 10.1046/j.1365-3083.1997.d01-108.x

Source DB:  PubMed          Journal:  Scand J Immunol        ISSN: 0300-9475            Impact factor:   3.487


  1 in total

1.  N-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid A: An imaging mass spectrometry study.

Authors:  Yukako Shintani-Domoto; Yuki Sugiura; Makiko Ogawa; Eiji Sugiyama; Hiroyuki Abe; Takashi Sakatani; Ryuji Ohashi; Tetsuo Ushiku; Masashi Fukayama
Journal:  PLoS One       Date:  2022-10-14       Impact factor: 3.752

  1 in total

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