Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Human Caspase 8 Protein expressed in Escherichia coli (E. coli) - ABIN2487286
Appukuttan, Kasseckert, Micoogullari, Flacke, Kumar, Woste, Abdallah, Pott, Reusch, Ladilov: Type 10 adenylyl cyclase mediates mitochondrial Bax translocation and apoptosis of adult rat cardiomyocytes under simulated ischaemia/reperfusion. in Cardiovascular research 2012
Show all 6 Pubmed References
Human Caspase 8 Protein expressed in Escherichia coli (E. coli) - ABIN2688831
Nicholson, Ali, Thornberry, Vaillancourt, Ding, Gallant, Gareau, Griffin, Labelle, Lazebnik: Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. in Nature 1995
Show all 3 Pubmed References
Human Caspase 8 Protein expressed in Escherichia coli (E. coli) - ABIN2688834
Patel, Gores, Kaufmann: The role of proteases during apoptosis. in FASEB journal : official publication of the Federation of American Societies for Experimental Biology 1996
Show all 3 Pubmed References
Furthermore, while activities to process procaspase-8 and procaspase-9 appeared in SAMDC (show AMD1 Proteins)-overexpressed apoptotic embryos, the activity to process procaspase-8 did not appear in p53 (show TP53 Proteins)-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 Proteins) 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 Proteins) triggered two caspase 8 activation pathways through the induction of RIP1 (show RALBP1 Proteins)-FADD (show FADD Proteins)-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 Proteins) 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 Proteins) and caspase-8 were observed, along with other molecules involved in the extrinsic apoptotic pathway such as Dapk1 (show DAPK1 Proteins), Traf3 (show TRAF3 Proteins), Tnsf12, Tnfrsf1A (show TNFRSF1A Proteins) and Ripk1 (show RIPK1 Proteins).
Results suggest that caspase-8 could regulate receptor-interacting protein 3 (RIP3 (show RIPK3 Proteins))-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 Proteins) activation in Intestinal epithelial cells (IECs) leads to cell expulsion and IL-18 (show IL18 Proteins) release, and implicate Caspase-8 in NLRC4 (show NLRC4 Proteins) inflammasome responses in vivo by generation of doubly deficient in Caspase-1 (show CASP1 Proteins) and Caspase-8.
ING4 (show ING4 Proteins) might suppress proliferation and enhance apoptosis in human malignant melanoma cells by activating Fas (show FAS Proteins)-induced apoptosis in a caspase-8-dependent 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 Proteins), 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 Proteins) (TRIF (show TRIM69 Proteins)) are regulated by autophagy and propose that pro-apoptotic signalling through TRIF (show TRIM69 Proteins)/RIPK1 (show RIPK1 Proteins)/caspase-8 occurs in fibrillary platforms.
Insertion genotype of CASP8 rs3834129 polymorphisms showed risk in CAD. CASP8 rs3769818 activates intronic cryptic donor.
Caspase-8 controls the secretion of inflammatory lysyl-tRNA synthetase (show KARS Proteins) in exosomes from colorectal cancer cells.
Fisetin inhibited Triple-Negative Breast Cancer Cells cell division and induced apoptosis, which was associated with mitochondrial membrane permeabilization and the activation of caspase-9 (show CASP9 Proteins) and caspase-8, as well as the cleavage of poly(ADP-ribose) polymerase-1 (show PARP1 Proteins).
Caspase-8 can serve in two distinct roles in response to TRAIL receptor engagement, as a scaffold for assembly of a Caspase-8-FADD-RIPK1 "FADDosome" complex, leading to NFkappaB-dependent inflammation, or as a protease that promotes apoptosis.
S. aureus-induced apoptosis in bovine mammary epithelial cells apoptosis was mitigated by caspase-3 (show CASP3 Proteins) 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 Proteins).
Nitric oxide-dependent increase in caspase-8 mRNA levels is associated with phosphorylation of STAT-1 (show STAT1 Proteins) at Ser (show SIGLEC1 Proteins)-727 and STAT1 (show STAT1 Proteins) 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 Proteins), IL-6 (show IL6 Proteins), IL-12p40, IL-1beta (show IL1B Proteins), and resulted in increased expression of the apoptosis initiator caspase-8 and bcl2L1 (show BCL2L1 Proteins).
Induction of apoptosis through targeted activation of caspase (show CASP3 Proteins) by tamoxifen (ATTAC(TM)) further expands the repertoire of genetic tools for conditional interrogation of cellular functions.
Targeted gene knockdown of TNFRSF1B (show TNFRSF1B Proteins) in zebrafish embryos results in the induction of a caspase-8, caspase-2 (show CASP2 Proteins) and P53 (show TP53 Proteins)-dependent apoptotic program in endothelial cells that bypasses caspase-3 (show CASP3 Proteins).
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