Human TNF-R (60kDa) FlowCytomix Simplex

Description: This FlowCytomix Simplex Kit is designed for the measurement of Human TNF-R (60kDa) in an immunoassay analyzed on a flow cytometer. Together with the FlowCytomix Human Basic Kit (cat. BMS8420FF), this kit can be used to detect TNF-R (60kDa) alone or can be multiplexed with other Simplex Kits to measure a variety of analytes.

This kit contains bead population A5.

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.

The present assay provides a simple, rapid, and highly sensitive method for the determination of soluble TNF-R (60 kDa) levels in body fluids or cell culture supernatants. This assay will help to clarify the possible diagnostic and prognostic value of circulating sTNF-R (60 kDa) in various neoplastic and inflammatory diseases.

References: Smith,C.A.; Davis,T.; Anderson,D.; Solam,L.; Beckmann,M.P.; Jerzy,R.; Dower,S.K.; Cosman,D.; Goodwin,R.G.. A receptor for tumor necrosis factor defines an unusual family of cellular and viral proteins. Science 1990;248:1019-1023. (Link)

Loetscher,H.; Pan,Y.C.; Lahm,H.W.; Gentz,R.; Brockhaus,M.; Tabuchi,H.; Lesslauer,W.. Molecular cloning and expression of the human 55 kd tumor necrosis factor receptor. Cell 1990;61:351-359. (Link)

Scheurich,P.; Thoma,B.; Ucer,U.; Pfizenmaier,K.. Immunoregulatory activity of recombinant human tumor necrosis factor (TNF)-alpha: induction of TNF receptors on human T cells and TNF-alpha-mediated enhancement of T cell responses. J.Immunol. 1987;138:1786-1790. (Link)

Schall,T.J.; Lewis,M.; Koller,K.J.; Lee,A.; Rice,G.C.; Wong,G.H.; Gatanaga,T.; Granger,G.A.; Lentz,R.; Raab,H.; .. Molecular cloning and expression of a receptor for human tumor necrosis factor. Cell 1990;61:361-370. (Link)

Aggarwal,B.B.; Eessalu,T.E.; Hass,P.E.. Characterization of receptors for human tumour necrosis factor and their regulation by gamma-interferon. Nature 1985;318:665-667. (Link)

Brockhaus,M.; Schoenfeld,H.J.; Schlaeger,E.J.; Hunziker,W.; Lesslauer,W.; Loetscher,H.. Identification of two types of tumor necrosis factor receptors on human cell lines by monoclonal antibodies. Proc.Natl.Acad.Sci.U.S.A 1990;87:3127-3131. (Link)

Adolf,G.R.; Apfler,I.. A monoclonal antibody-based enzyme immunoassay for quantitation of human tumor necrosis factor binding protein I, a soluble fragment of the 60 kDa TNF receptor, in biological fluids. J.Immunol.Methods 1991;143:127-136. (Link)

Creasey,A.A.; Yamamoto,R.; Vitt,C.R.. A high molecular weight component of the human tumor necrosis factor receptor is associated with cytotoxicity. Proc.Natl.Acad.Sci.U.S.A 1987;84:3293-3297. (Link)

Tsujimoto,M.; Yip,Y.K.; Vilcek,J.. Tumor necrosis factor: specific binding and internalization in sensitive and resistant cells. Proc.Natl.Acad.Sci.U.S.A 1985;82:7626-7630. (Link)

Kull,F.C.,Jr.; Jacobs,S.; Cuatrecasas,P.. Cellular receptor for 125I-labeled tumor necrosis factor: specific binding, affinity labeling, and relationship to sensitivity. Proc.Natl.Acad.Sci.U.S.A 1985;82:5756-5760. (Link)

Rubin,B.Y.; Anderson,S.L.; Sullivan,S.A.; Williamson,B.D.; Carswell,E.A.; Old,L.J.. High affinity binding of 125I-labeled human tumor necrosis factor (LuKII) to specific cell surface receptors. J.Exp.Med. 1985;162:1099-1104. (Link)

Paul,N.L.; Ruddle,N.H.. Lymphotoxin. Annu.Rev.Immunol. 1988;6:407-438. (Link)

Beutler,B.; Mahoney,J.; Le,Trang N.; Pekala,P.; Cerami,A.. Purification of cachectin, a lipoprotein lipase-suppressing hormone secreted by endotoxin-induced RAW 264.7 cells. J.Exp.Med. 1985;161:984-995. (Link)

Baglioni,C.; McCandless,S.; Tavernier,J.; Fiers,W.. Binding of human tumor necrosis factor to high affinity receptors on HeLa and lymphoblastoid cells sensitive to growth inhibition. J.Biol.Chem. 1985;260:13395-13397. (Link)

Scheurich,P.; Ucer,U.; Kronke,M.; Pfizenmaier,K.. Quantification and characterization of high-affinity membrane receptors for tumor necrosis factor on human leukemic cell lines. Int.J.Cancer 1986;38:127-133. (Link)

Olsson,I.; Lantz,M.; Nilsson,E.; Peetre,C.; Thysell,H.; Grubb,A.; Adolf,G.. Isolation and characterization of a tumor necrosis factor binding protein from urine. Eur.J.Haematol. 1989;42:270-275. (Link)

Munker,R.; DiPersio,J.; Koeffler,H.P.. Tumor necrosis factor: receptors on hematopoietic cells. Blood 1987;70:1730-1734. (Link)

Himmler,A.; Maurer-Fogy,I.; Kronke,M.; Scheurich,P.; Pfizenmaier,K.; Lantz,M.; Olsson,I.; Hauptmann,R.; Stratowa,C.; Adolf,G.R.. Molecular cloning and expression of human and rat tumor necrosis factor receptor chain (p60) and its soluble derivative, tumor necrosis factor-binding protein. DNA Cell Biol. 1990;9:705-715. (Link)

Thoma,B.; Grell,M.; Pfizenmaier,K.; Scheurich,P.. Identification of a 60-kD tumor necrosis factor (TNF) receptor as the major signal transducing component in TNF responses. J.Exp.Med. 1990;172:1019-1023. (Link)

Hohmann,H.P.; Remy,R.; Brockhaus,M.; van Loon,A.P.. Two different cell types have different major receptors for human tumor necrosis factor (TNF alpha). J.Biol.Chem. 1989;264:14927-14934. (Link)