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Immunohistochemical staining with newly developed metallothionein fragment antibodies against NH 2 ‐terminal, middle‐regional and COOH‐terminal peptides in rabbits
Author(s) -
Nakazato Kyoumi,
Nakajima Katsuyuki,
Kusakabe Takahiko,
Suzuki Keiji,
Nagamine Takeaki
Publication year - 2008
Publication title -
pathology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.73
H-Index - 74
eISSN - 1440-1827
pISSN - 1320-5463
DOI - 10.1111/j.1440-1827.2008.02308.x
Subject(s) - immunohistochemistry , terminal (telecommunication) , metallothionein , antibody , staining , fragment (logic) , pathology , microbiology and biotechnology , chemistry , biology , medicine , biochemistry , immunology , computer science , gene , telecommunications , programming language
Metallothionein (MT) has been reported to play important physiological roles in the human body, but the distribution and significance of MT is not fully understood. In order to analyze MT expression, three kinds of polyclonal MT fragment antibodies were developed against NH 2 ‐terminal, middle regional and COOH‐terminal peptide followed by human MT‐IA amino acid sequence in rabbits. The characteristics of these antibodies were studied using competitive immunoassay and immunohistochemical staining. The NH 2 ‐terminal antibody (anti‐MT‐N) had the strongest and clearest immunoreactivity to human and mouse tissues, while COOH‐terminal antibody (anti‐MT‐C) showed species difference because of the 4 amino acid difference in the MT fragment peptide between human and mouse. No reactivity was detected using middle regional residue antibody (anti‐MT‐M) both on competitive immunoassay and on immunostaining. These results suggest that anti‐MT‐N is the most applicable antibody to use for immunohistochemistry in human, mouse and other specimens.