Molecular cloning and expression of a receptor for human tumor necrosis factor.
作者： Thomas J. Schall , Martyn Lewis , Kerry J. Koller , Angela Lee , Glenn C. Rice
DOI: 10.1016/0092-8674(90)90816-W
关键词: Peptide sequence 、 Cell surface receptor 、 Biology 、 Molecular cloning 、 Tumor necrosis factor alpha 、 Expression vector 、 Binding protein 、 Molecular biology 、 Receptor 、 Complementary DNA
摘要: A human tumor necrosis factor (TNF) binding protein from serum of cancer patients was purified to homogeneity and partially sequenced. Synthetic DNA probes based on amino acid sequence information were used isolate cDNA clones encoding a receptor for TNF. The TNF (TNF-R) is 415 polypeptide with single membrane-spanning region. extracellular cysteine-rich domain the TNF-R homologous nerve growth B cell activation Bp50. Human embryonic kidney cells transfected expression vector specifically bind both 125I-labeled biotinylated TNF-alpha. Unlabeled TNF-alpha TNF-beta equally effective at displacing labeled expressing cells. Northern analysis indicates species mRNA in variety types. Therefore, soluble found probably proteolytically derived TNF-R.
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