A new monoclonal antibody, 4-1a,that binds to the amino terminus of human lipoprotein lipase |
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Authors: | André Bensadoun,Charlene D. Mottler,Chris Pelletier,Daniel Wu,Jane J. Seo,Calvin S. Leung,Oludotun Adeyo,Chris N. Goulbourne,Peter Gin,Loren G. Fong,Stephen G. Young,Anne P. Beigneux |
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Affiliation: | 1. Division of Nutritional Science, Cornell University, Ithaca, NY 14853, USA;2. Department of Medicine, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA;3. Department of Human Genetics, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA |
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Abstract: | Lipoprotein lipase (LPL) has been highly conserved through vertebrate evolution, making it challenging to generate useful antibodies. Some polyclonal antibodies against LPL have turned out to be nonspecific, and the available monoclonal antibodies (Mabs) against LPL, all of which bind to LPL's carboxyl terminus, have drawbacks for some purposes. We report a new LPL-specific monoclonal antibody, Mab 4-1a, which binds to the amino terminus of LPL (residues 5–25). Mab 4-1a binds human and bovine LPL avidly; it does not inhibit LPL catalytic activity nor does it interfere with the binding of LPL to heparin. Mab 4-1a does not bind to human hepatic lipase. Mab 4-1a binds to GPIHBP1-bound LPL and does not interfere with the ability of the LPL–GPIHBP1 complex to bind triglyceride-rich lipoproteins. Mab 4-1a will be a useful reagent for both biochemists and clinical laboratories. |
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Keywords: | Lipoprotein lipase Monoclonal antibody GPIHBP1 Triglyceride Hyperlipidemia |
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