TY - JOUR
T1 - Establishment of a monoclonal antibody for human LXRα
T2 - Detection of LXRα protein expression in human macrophages
AU - Watanabe, Yuichiro
AU - Tanaka, Toshiya
AU - Uchiyama, Yasutoshi
AU - Takeno, Tetsu
AU - Izumi, Akashi
AU - Yamashita, Hisahiko
AU - Kumakura, Junko
AU - Iwanari, Hiroko
AU - Shu-Ying, Jiang
AU - Naito, Makoto
AU - Mangelsdorf, David J.
AU - Hamakubo, Takao
AU - Kodama, Tatsuhiko
PY - 2003/5/9
Y1 - 2003/5/9
N2 - Liver X activated receptor alpha (LXRα) 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 LXRα protein level in the cell is low and the LXRα protein itself is very hard to detect. We have previously reported that the mRNA for LXRα is highly expressed in human cultured macrophages. In order to confirm the presence of the LXRα protein in the human macrophage, we have established a monoclonal antibody against LXRα, K-8607. The binding of mAb K-8607 to the human LXRα 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-LXRα antibody should prove to be a useful tool in the analysis of the human LXRα protein.
AB - Liver X activated receptor alpha (LXRα) 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 LXRα protein level in the cell is low and the LXRα protein itself is very hard to detect. We have previously reported that the mRNA for LXRα is highly expressed in human cultured macrophages. In order to confirm the presence of the LXRα protein in the human macrophage, we have established a monoclonal antibody against LXRα, K-8607. The binding of mAb K-8607 to the human LXRα 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-LXRα antibody should prove to be a useful tool in the analysis of the human LXRα protein.
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U2 - 10.1186/1478-1336-1-1
DO - 10.1186/1478-1336-1-1
M3 - Article
C2 - 12904258
AN - SCOPUS:2442658405
SN - 1478-1336
VL - 1
JO - Nuclear Receptor
JF - Nuclear Receptor
M1 - 1
ER -