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Patil, Kim, Jayaprakasha: Berberine induces apoptosis in breast cancer cells (MCF-7) through mitochondrial-dependent pathway. in European journal of pharmacology 2010
Show all 35 Pubmed References
Anginot, Espeli, Chasson, Mancini, Schiff: Galectin 1 modulates plasma cell homeostasis and regulates the humoral immune response. in Journal of immunology (Baltimore, Md. : 1950) 2013
Show all 16 Pubmed References
Patel, Wilson, ODea, Takata: TNF-induced death signaling triggers alveolar epithelial dysfunction in acute lung injury. in Journal of immunology (Baltimore, Md. : 1950) 2013
Show all 11 Pubmed References
Abdel-Latif, Murray, Renberg, ONeill, Porter, Jensen, Johnson: Cell death in bovine parvovirus-infected embryonic bovine tracheal cells is mediated by necrosis rather than apoptosis. in The Journal of general virology 2006
Show all 6 Pubmed References
Teachey, Obzut, Axsom, Choi, Goldsmith, Hall, Hulitt, Manno, Maris, Rhodin, Sullivan, Brown, Grupp: Rapamycin improves lymphoproliferative disease in murine autoimmune lymphoproliferative syndrome (ALPS). in Blood 2006
Rat (Rattus) Caspase 8 ELISA Kit for Sandwich ELISA - ABIN416145
Abdelkader, Safar, Salem: Ursodeoxycholic Acid Ameliorates Apoptotic Cascade in the Rotenone Model of Parkinson's Disease: Modulation of Mitochondrial Perturbations. in Molecular neurobiology 2015
Furthermore, while activities to process procaspase-8 and procaspase-9 appeared in SAMDC (show AMD1 ELISA Kits)-overexpressed apoptotic embryos, the activity to process procaspase-8 did not appear in p53 (show TP53 ELISA Kits)-overexpressed apoptotic embryos.
tail regression at metamorphosis implicates an apoptotic pathway inducible by T(3) hormone in an organ autonomous manner and involving the cell death executioners BH3 interacting domain death agonist (show BID ELISA Kits) and Caspases-2 and -8
Results illustrate the temporal and spatial activation of caspase-8 and -3 in microglia/macrophages occurring upon ischemic stroke and suggest that the expression of these caspases could be used in neuropathological diagnostic work.
inhibition of TAK1 (show NR2C2 ELISA Kits) triggered two caspase 8 activation pathways through the induction of RIP1 (show RALBP1 ELISA Kits)-FADD (show FADD ELISA Kits)-caspase 8 complex as well as FLIP cleavage/degradation.
this study identifies a crucial role for caspase-8 in the development of allergic airway inflammation
Prolonged treatment of human PMNs or mice bone marrow derived neutrophils (BMDN) with nitric oxide led to enhanced reactive oxygen species generation, caspase-8/caspase-3 (show CASP3 ELISA Kits) cleavage, reduced mitochondrial membrane potential and finally cellular apoptosis.
caspase-8-dependent apoptosis was linked to hepatocellular carcinoma development.
Statistically significant increases in the expression of Fas (show FAS ELISA Kits) and caspase-8 were observed, along with other molecules involved in the extrinsic apoptotic pathway such as Dapk1 (show DAPK1 ELISA Kits), Traf3 (show TRAF3 ELISA Kits), Tnsf12, Tnfrsf1A (show TNFRSF1A ELISA Kits) and Ripk1 (show RIPK1 ELISA Kits).
Results suggest that caspase-8 could regulate receptor-interacting protein 3 (RIP3 (show RIPK3 ELISA Kits))-mediated necroptosis.
we show that caspase-8 activity promotes cell-intrinsic cytokine expression, independent of its role in cell death in response to Yersinia infection
Data indicate that NLRC4 (show NLRC4 ELISA Kits) activation in Intestinal epithelial cells (IECs) leads to cell expulsion and IL-18 (show IL18 ELISA Kits) release, and implicate Caspase-8 in NLRC4 (show NLRC4 ELISA Kits) inflammasome responses in vivo by generation of doubly deficient in Caspase-1 (show CASP1 ELISA Kits) and Caspase-8.
ING4 (show ING4 ELISA Kits) might suppress proliferation and enhance apoptosis in human malignant melanoma cells by activating Fas (show FAS ELISA Kits)-induced apoptosis in a caspase-8-dependent pathway.
The procaspase-8 Q482H mutation in AML (show RUNX1 ELISA Kits) patients abolishes caspase-8-mediated apoptosis by impairing procaspase-8 dimerization.
These findings suggest that intracellular cholesterol level affects TMZ treatment of GBM mediated via a DR5 (show TNFRSF10B ELISA Kits)-caspase-8 mechanism.
study shows genetic association of rare variants in CASP8 with Alzheimer's disease and proposes a mechanism of action mediated by decreased enzyme activity; for two CASP8 variants, p.K148R and p.I298V, the association remained significant in a large combined sample
Knockout (KO) or knockdown of caspase-8, CD95 (show FAS ELISA Kits) or FADD (show FADD ELISA Kits) prevents activation of Plk3 (show PLK3 ELISA Kits) upon CD95 (show FAS ELISA Kits) stimulation, suggesting a requirement of a functional death-inducing signaling complex for Plk3 (show PLK3 ELISA Kits) activation.
CASP8: rs1045494 (C > T), PIK3R1: rs3756668 (A > G) and CASP7 (show CASP7 ELISA Kits): rs4353229 (T > C), were associated with longer overall survival in limited disease-small cell lung cancer patients after chemoradiotherapy
SP-D (show SFTPD ELISA Kits) increases the formation of nuclear and membrane blebs. Inhibition of caspase-8 confirms the effect of SP-D (show SFTPD ELISA Kits) is unique to the caspase-8 pathway.
This is the first report, showing negative and independent prognostic impact of the CASP8 -652 6N Del and the 302His variant for breast cancer.
The C-terminal helical conformation of Bax (show BAX ELISA Kits), not its primary sequence, appears to be critical for CASP8 recruitment and activation culminating in cell death.
Data suggest that pro-death signals through TIR-domain-containing adapter-inducing interferon-beta (show IFNB1 ELISA Kits) (TRIF (show TRIM69 ELISA Kits)) are regulated by autophagy and propose that pro-apoptotic signalling through TRIF (show TRIM69 ELISA Kits)/RIPK1 (show RIPK1 ELISA Kits)/caspase-8 occurs in fibrillary platforms.
S. aureus-induced apoptosis in bovine mammary epithelial cells apoptosis was mitigated by caspase-3 (show CASP3 ELISA Kits) and caspase-8 inhibitors, suggesting that apoptosis is initiated via caspase-8 activation.
Endothelial cell apoptosis by H. somnus-activated platelets required activation of both caspase-8 and caspase-9 (show CASP9 ELISA Kits).
Nitric oxide-dependent increase in caspase-8 mRNA levels is associated with phosphorylation of STAT-1 (show STAT1 ELISA Kits) at Ser (show SIGLEC1 ELISA Kits)-727 and STAT1 (show STAT1 ELISA Kits) binding to the caspase-8 promoter in cultured lung endothelial cells.
Data show that cysteine significantly reduced the expression of pro-inflammatory cytokines, including TNF-alpha (show TNF ELISA Kits), IL-6 (show IL6 ELISA Kits), IL-12p40, IL-1beta (show IL1B ELISA Kits), and resulted in increased expression of the apoptosis initiator caspase-8 and bcl2L1 (show BCL2L1 ELISA Kits).
Induction of apoptosis through targeted activation of caspase (show CASP3 ELISA Kits) by tamoxifen (ATTAC(TM)) further expands the repertoire of genetic tools for conditional interrogation of cellular functions.
Targeted gene knockdown of TNFRSF1B (show TNFRSF1B ELISA Kits) in zebrafish embryos results in the induction of a caspase-8, caspase-2 (show CASP2 ELISA Kits) and P53 (show TP53 ELISA Kits)-dependent apoptotic program in endothelial cells that bypasses caspase-3 (show CASP3 ELISA Kits).
These results show that zebrafish casp8 has a structure and function similar to mammalian CASP8 orthologs and the role of caspase-8 in the apoptotic signal pathway has been conserved over at least 450 million years of vertebrate evolution.
This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. This protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have been described, although not all variants have had their full-length sequences determined.
, xcaspase 8
, death related ced-3/Nedd2-like protein
, caspase 8, apoptosis-related cysteine peptidase
, caspase 8
, DEATH effector domain caspase
, Fas-linked ICE-like protease
, FADD-homologous ICE/CED-3-like protease
, FADD-like ICE
, ICE-like apoptotic protease 5
, MACH-alpha-1/2/3 protein
, MACH-beta-1/2/3/4 protein
, MORT1-associated ced-3 homolog
, apoptotic cysteine protease
, apoptotic protease Mch-5
, caspase 8, apoptosis-related cysteine protease
, cysteine protease