1992年2月
ASSOCIATION OF RECOMBINANT SOLUBLE IL-6-SIGNAL TRANSDUCER, GP130, WITH A COMPLEX OF IL-6-RECEPTOR AND SOLUBLE IL-6-RECEPTOR, AND ESTABLISHMENT OF AN ELISA FOR SOLUBLE GP130
IMMUNOLOGY LETTERS
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- 巻
- 31
- 号
- 2
- 開始ページ
- 123
- 終了ページ
- 130
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/0165-2478(92)90138-E
- 出版者・発行元
- ELSEVIER SCIENCE BV
IL-6 mediates its pleiotropic functions through two membrane proteins, a ligand-binding molecule (IL-6 receptor, IL-6R) and a non-ligand-binding signal transducer (gp130). Starting with a previously isolated cDNA clone encoding human gp130, recombinant soluble gp130 (sgp130) lacking the transmembrane and cytoplasmic regions was expressed in COS7 cells or CHO cells. sgp130 could associate with a complex of IL-6 and soluble IL-6R (sIL-6R), also lacking transmembrane and cytoplasmic regions. This indicated that extracellular region of gp130 was responsible for the association with IL-6R which was occupied by IL-6. An enzyme-linked immunosorbent assay (ELISA) for the quantitation of sgp130 was established, which was based on the interaction of sgp130 with the complex of IL-6 and SIL-6R and could detect sgp130 as low as 1 ng/ml.
- リンク情報
- ID情報
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- DOI : 10.1016/0165-2478(92)90138-E
- ISSN : 0165-2478
- Web of Science ID : WOS:A1992GY33900005