Establishment of a monoclonal antibody for human LXR alpha : Detection of LXR alpha

• Published in: Nuclear receptor 2003-01, Vol.1
• Main Authors: Watanabe, Yuichiro, Tanaka, Toshiya, Uchiyama, Yasutoshi, Takeno, Tetsu, Izumi, Akashi, Yamashita, Hisahiko, Kumakura, Junko, Iwanari, Hiroko, Shu-Ying, Jiang, Naito, Makoto, Mangelsdorf, David J, Hamakubo, Takao, Kodama, Tatsuhiko
• Format: Article
• Language: English
• ISSN: 1478-1336; 1478-1336
• DOI: 10.1186/1478-1336-1-1

Liver X activated receptor alpha (LXR alpha ) forms a functional dimeric nuclear receptor with RXR that regulates the metabolism of several important lipids, including cholesterol and bile acids. As compared with RXR, the LXR protein level in the cell is low and the LXR protein itself is very hard to detect. We have previously reported that the mRNA for LXR is highly expressed in human cultured macrophages. In order to confirm the presence of the LXR protein in the human macrophage, we have established a monoclonal antibody against LXR, K-8607. The binding of mAb K-8607 to the human LXR protein was confirmed by a wide variety of different techniques, including immunoblotting, immunohistochemistry, and electrophoretic mobility shift assay (EMSA). By immunoblotting with this antibody, the presence of native LXR protein in primary cultured human macrophage was demonstrated, as was its absence in human monocytes. This monoclonal anti-LXR antibody should prove to be a useful tool in the analysis of the human LXR protein.