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Cross‐species reactivity of a monoclonal antibody against glutathione S‐transferase fusion protein of human β2‐adrenergic receptor
Author(s) -
Shin Chan Young,
Kang Sukjo,
Song Miryoung,
Park Kyu Hwan,
Seo Dong Ook,
Cheong Jae Hoon,
Ko Kwang Ho
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800202582
Subject(s) - monoclonal antibody , microbiology and biotechnology , receptor , western blot , antibody , fusion protein , biology , chemistry , biochemistry , recombinant dna , immunology , gene
The purpose of the present study was to produce and characterize a monoclonal antibody against human β2‐adrenergic receptor. Male BALB/c mice were immunized with glutathione S‐transferase (GST) fusion protein of the C‐terminal portion of the human β2‐adrenergic receptor which was expressed in E.Coli. The immunized splenocytes were fused with myeloma SP2/0‐Ag14 cells and the resulting monoclonal antibody was named as mAbβC02. The monoclonal antibody βC02 was determined as IgM subtype and then purified by anti‐mouse IgM‐agarose affinity chromatography. The results of ELISA, Western blot, and immunocytochemistry showed that mAbβC02 recognized human β2‐adrenergic receptor in the β2‐adrenergic receptor‐GST fusion protein and human epidermoid carcinoma cell line A431 with highly specific immunoreactivity. In addition, mAbβC02 showed cross‐species reactivity against β‐adrenergic receptor of hamster lung and rat brain as revealed by Western blot and immunohistochemistry. The monoclonal antibody βC02 may provide useful tools for the study of the β‐adrenergic receptor of human and other species including rats.