Human Caspase-8 Platinum ELISA

Also known as: MACH, FADD-homologous ICE/CED-3-like protease

RUO: For Research Use Only. Not for use in diagnostic procedures.

SKU# BMS2024*

Cat. No. Size
BMS2024 96 tests
BMS2024TEN 10 x 96 tests
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Data for Human Caspase-8 Platinum ELISA.

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  • Data for Human Caspase-8 Platinum ELISA.
Description

Description: The human Caspase-8 ELISA is an enzyme-linked immunosorbent assay for the quantitative detection of human Caspase-8. The human Caspase-8 ELISA is for research use only. Not for diagnostic or therapeutic procedures.

Caspases are the executioners of apoptosis. These cysteine protease family consists of more than 10 related members characterized by almost absolute specificity for aspartic acid in the P1 position. Caspases are synthesized as inactive proenzymes comprising an N-terminal peptide together with one large and one small subunit. Activation of caspases during apoptosis results in the cleavage of critical cellular substrates so precipitating the dramatic morphological changes of apoptosis.

Caspase-8 has been reported to have additional functions unrelated to cell death. It is required for T-cell homeostasis, proliferation, and cell activation.

Details
Reactivity Human
Sample Volume 50 uL
Suitable Sample Types cell culture supernatant, cell lysate, serum
Sensitivity 0.10 ng/mL
Standard Curve Range 0.16 - 10.0 ng/mL
Components Aluminium pouch(es) with a Microwell Plate coated with monoclonal antibody to human Caspase-8
anti-human Caspase-8 polyclonal (rabbit) Detection Antibody
Anti-rabbit-IgG-HRP
Human Caspase-8 Standard lyophilized, 20.00 ng/ml upon reconstitution
Sample Diluent
Assay Buffer Concentrate 20x (PBS with 1% Tween 20 and 10% BSA)
Wash Buffer Concentrate 20x (PBS with 1% Tween 20)
Lysis Buffer 10x
Substrate Solution (tetramethyl-benzidine)
Stop Solution (1M Phosphoric acid)
Blue-Dye
Green-Dye
Red-Dye
Adhesive Films
Reported Applications ELISA
Documentation

For complete product information, please download the TDS or IFU document.

TDS Link Download TDS
Additional Formats
References

References: Thome,M.; Tschopp,J.. Regulation of lymphocyte proliferation and death by FLIP 122. Nat.Rev.Immunol. 2001;1:50-58. (Link)

Krueger,A.; Schmitz,I.; Baumann,S.; Krammer,P.H.; Kirchhoff,S.. Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex 69. J.Biol.Chem. 2001;276:20633-20640. (Link)

Tai,T.S.; Fang,L.W.; Lai,M.Z.. c-FLICE inhibitory protein expression inhibits T-cell activation. Cell Death.Differ. 2004;11:69-79. (Link)

Wajant,H.. Targeting the FLICE Inhibitory Protein (FLIP) in cancer therapy. Mol Interv. 2003;3:124-127. (Link)

Medema,J.P.; Toes,R.E.; Scaffidi,C.; Zheng,T.S.; Flavell,R.A.; Melief,C.J.; Peter,M.E.; Offringa,R.; Krammer,P.H.. Cleavage of FLICE (caspase-8) by granzyme B during cytotoxic T lymphocyte-induced apoptosis. Eur.J.Immunol. 1997;27:3492-3498. (Link)

Medema,J.P.; Scaffidi,C.; Kischkel,F.C.; Shevchenko,A.; Mann,M.; Krammer,P.H.; Peter,M.E.. FLICE is activated by association with the CD95 death-inducing signaling complex (DISC) 89. EMBO J. 1997;16:2794-2804. (Link)

de,Jonge N.; van Wichen,D.F.; van,Kuik J.; Kirkels,H.; Lahpor,J.R.; Gmelig-Meyling,F.H.; van den Tweel,J.G.; de Weger,R.A.. Cardiomyocyte death in patients with end-stage heart failure before and after support with a left ventricular assist device: low incidence of apoptosis despite ubiquitous mediators. J.Heart Lung Transplant. 2003;22:1028-1036. (Link)

Okano,H.; Shiraki,K.; Inoue,H.; Kawakita,T.; Yamanaka,T.; Deguchi,M.; Sugimoto,K.; Sakai,T.; Ohmori,S.; Fujikawa,K.; Murata,K.; Nakano,T.. Cellular FLICE/caspase-8-inhibitory protein as a principal regulator of cell death and survival in human hepatocellular carcinoma. Lab Invest 2003;83:1033-1043. (Link)

You,K.R.; Shin,M.N.; Park,R.K.; Lee,S.O.; Kim,D.G.. Activation of caspase-8 during N-(4-hydroxyphenyl)retinamide-induced apoptosis in Fas-defective hepatoma cells. Hepatology 2001;34:1119-1127. (Link)

Kim,P.K.; Mahidhara,R.; Seol,D.W.. The role of caspase-8 in resistance to cancer chemotherapy. Drug Resist.Updat. 2001;4:293-296. (Link)

Kuwana,T.; Smith,J.J.; Muzio,M.; Dixit,V.; Newmeyer,D.D.; Kornbluth,S.. Apoptosis induction by caspase-8 is amplified through the mitochondrial release of cytochrome c. J.Biol.Chem. 1998;273:16589-16594. (Link)

Wesselborg,S.; Engels,I.H.; Rossmann,E.; Los,M.; Schulze-Osthoff,K.. Anticancer drugs induce caspase-8/FLICE activation and apoptosis in the absence of CD95 receptor/ligand interaction. Blood 1999;93:3053-3063. (Link)

Hennino,A.; Berard,M.; Krammer,P.H.; Defrance,T.. FLICE-inhibitory protein is a key regulator of germinal center B cell apoptosis. J.Exp.Med. 2001;193:447-458. (Link)

Nitobe,J.; Yamaguchi,S.; Okuyama,M.; Nozaki,N.; Sata,M.; Miyamoto,T.; Takeishi,Y.; Kubota,I.; Tomoike,H.. Reactive oxygen species regulate FLICE inhibitory protein (FLIP) and susceptibility to Fas-mediated apoptosis in cardiac myocytes. Cardiovasc.Res. 2003;57:119-128. (Link)

Grenet,J.; Teitz,T.; Wei,T.; Valentine,V.; Kidd,V.J.. Structure and chromosome localization of the human CASP8 gene. Gene 1999;226:225-232. (Link)

Scaffidi,C.; Medema,J.P.; Krammer,P.H.; Peter,M.E.. FLICE is predominantly expressed as two functionally active isoforms, caspase-8/a and caspase-8/b. J.Biol.Chem. 1997;272:26953-26958. (Link)

Micheau,O.. Cellular FLICE-inhibitory protein: an attractive therapeutic target?. Expert.Opin.Ther.Targets. 2003;7:559-573. (Link)

Martin,D.A.; Siegel,R.M.; Zheng,L.; Lenardo,M.J.. Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHalpha1) death signal. J.Biol.Chem. 1998;273:4345-4349. (Link)

Boatright,K.M.; Deis,C.; Denault,J.B.; Sutherlin,D.P.; Salvesen,G.S.. Activation of caspases-8 and -10 by FLIP(L). Biochem.J. 2004;382:651-657. (Link)

Mezzanzanica,D.; Balladore,E.; Turatti,F.; Luison,E.; Alberti,P.; Bagnoli,M.; Figini,M.; Mazzoni,A.; Raspagliesi,F.; Oggionni,M.; Pilotti,S.; Canevari,S.. CD95-mediated apoptosis is impaired at receptor level by cellular FLICE-inhibitory protein (long form) in wild-type p53 human ovarian carcinoma. Clin.Cancer Res. 2004;10:5202-5214. (Link)

Engels,I.H.; Stepczynska,A.; Stroh,C.; Lauber,K.; Berg,C.; Schwenzer,R.; Wajant,H.; Janicke,R.U.; Porter,A.G.; Belka,C.; Gregor,M.; Schulze-Osthoff,K.; Wesselborg,S.. Caspase-8/FLICE functions as an executioner caspase in anticancer drug-induced apoptosis 38. Oncogene 2000;19:4563-4573. (Link)

Chou,K.C.; Jones,D.; Heinrikson,R.L.. Prediction of the tertiary structure and substrate binding site of caspase-8. FEBS Lett. 1997;419:49-54. (Link)

Dutton,A.; O'Neil,J.D.; Milner,A.E.; Reynolds,G.M.; Starczynski,J.; Crocker,J.; Young,L.S.; Murray,P.G.. Expression of the cellular FLICE-inhibitory protein (c-FLIP) protects Hodgkin's lymphoma cells from autonomous Fas-mediated death. Proc.Natl.Acad.Sci.U.S.A 2004;101:6611-6616. (Link)


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