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Caspase 8 Antibody (PA5-119007) in IHC (P)
Immunohistochemistry analysis of Caspase 8 in paraffin-embedded Human Pancreatic cancer tissue. Samples were incubated with polyclonal antibody (Product # PA5-119007) at a dilution of 10 µg/mL, followed by HRP-Linked Caprine Anti-Rabbit IgG using a dilution of 2 µg/mL.
Product Details
PA5-119007
Applications
Tested Dilution
Publications
Product Specifications
Species Reactivity
Human
Host/Isotype
Rabbit
/ IgG
Class
Polyclonal
Type
Antibody
Immunogen
Recombinant protein Caspase 8. The antigen corresponds to amino acid range 7-201 of the target protein.
Conjugate
Form
Liquid
Concentration
1.0 mg/mL
Purification
Antigen affinity chromatography
Storage buffer
PBS with 50% glycerol
Contains
0.05% ProClin 300
Storage conditions
-20°C
Shipping conditions
Wet ice
RRID
AB_2903507
Target Information
Caspase 8 (CASP8) is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases play a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a pro-domain, 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. Caspase 8 is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of Caspase 8 suggests that it may interact with Fas-interacting protein FADD. Caspase 8 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. Caspase 8 binds to the death effector domain (DED) of FADD through an analogous DED domain present in tandem in the pro-form of the Caspase 8 protein. Activated Caspase 8 then activates other downstream caspases including Caspase 9, thereby committing the cell to undergo apoptosis. In addition, Caspase 8 also reacts with Jurkat cells and Tonsil. Overexpression of Caspase 8 induces apoptosis, which can be blocked by inhibitors specific for the ICE family. Many alternatively spliced transcript variants encoding different isoforms have been described for Caspase 8, however, not all variants have had their full-length sequences determined.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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Bioinformatics
Protein Aliases: Apoptotic cysteine protease; Apoptotic protease Mch-5; CAP4; CASP-8; caspase 8, apoptosis-related cysteine peptidase; caspase 8, apoptosis-related cysteine protease; Caspase-8; Caspase-8 precursor; Caspase8; EC 3.4.22.61; FADD-homologous ICE/CED-3-like protease; FADD-like ICE; FLICE; FLJ17672; ICE-like apoptotic protease 5; ICE8; MACH; MACH-alpha-1/2/3 protein; MACH-beta-1/2/3/4 protein; MGC78473; MORT1-associated ced-3 homolog; OTTHUMP00000163720; OTTHUMP00000165063; OTTHUMP00000206557; OTTHUMP00000206581
Gene Aliases: ALPS2B; CAP4; Casp-8; CASP8; FLICE; MACH; MCH5
UniProt ID: (Human) Q14790
Entrez Gene ID: (Human) 841
cysteine-type endopeptidase activity
death receptor binding
tumor necrosis factor receptor binding
protein binding
peptidase activity
cysteine-type peptidase activity
ubiquitin protein ligase binding
protein complex binding
death effector domain binding
identical protein binding
scaffold protein binding
cysteine-type endopeptidase activity involved in apoptotic process
cysteine-type endopeptidase activity involved in apoptotic signaling pathway
protease
proteolysis
apoptotic process
activation of cysteine-type endopeptidase activity involved in apoptotic process
cellular component disassembly involved in execution phase of apoptosis
cell surface receptor signaling pathway
response to cold
regulation of tumor necrosis factor-mediated signaling pathway
regulation of necrotic cell death
natural killer cell activation
macrophage differentiation
response to cobalt ion
response to estradiol
response to lipopolysaccharide
response to tumor necrosis factor
TRIF-dependent toll-like receptor signaling pathway
TRAIL-activated apoptotic signaling pathway
suppression by virus of host cysteine-type endopeptidase activity involved in apoptotic process
T cell activation
B cell activation
positive regulation of I-kappaB kinase/NF-kappaB signaling
negative regulation of I-kappaB kinase/NF-kappaB signaling
response to ethanol
positive regulation of macrophage differentiation
positive regulation of proteolysis
response to antibiotic
protein heterooligomerization
proteolysis involved in cellular protein catabolic process
syncytiotrophoblast cell differentiation involved in labyrinthine layer development
nucleotide-binding oligomerization domain containing signaling pathway
cellular response to mechanical stimulus
cellular response to organic cyclic compound
death-inducing signaling complex assembly
apoptotic signaling pathway
extrinsic apoptotic signaling pathway
execution phase of apoptosis
activation of cysteine-type endopeptidase activity
activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway
positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway
regulation of extrinsic apoptotic signaling pathway via death domain receptors
negative regulation of extrinsic apoptotic signaling pathway via death domain receptors
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