Description: The monoclonal antibody TBP-1 recognizes Tumor Necrosis Factor Receptor type I (TNF-RI)
TNF-receptors have been demonstrated on a wide variety of human somatic cells including fibroblasts, endothelial cells, adipocytes, liver membranes, granulocytes and several tumor cell lines. Based on gel filtration experiments the receptor appears to be a complex of different proteins with a molecular weight of 350 kDa. In a variety of cell lines two different types of TNF receptors with 75-80 and 55-60 kDa respectively have been identified. The cDNAs encoding the two different TNF receptors have been cloned. The exact mechanism of signal transduction after binding of TNF to the receptor is still unclear. The extracellular fragment of the 60 kDa TNF receptor, with a molecular mass of about 30 kDa was purified, partially sequenced, and the respective cDNA was cloned. This TNF binding protein is liberated from the intact molecule by proteolytic cleavage and comprises most of the extracellular portion of the receptor, including all three N-glycosylation sites.
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