Invitrogen

Caspase 8 Polyclonal Antibody

View all (39) Caspase 8 antibodies

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Datasheet
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Datasheet
Protocols
Questions & Answers

Product Details

PA5-13498

Applications
Tested Dilution
Publications

Western Blot (WB)

1:2,000
-

Flow Cytometry (Flow)

1:25
-
Product Specifications

Species Reactivity

Human, Mouse

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

KLH conjugated synthetic peptide between 432-461 amino acids from the C-terminal region of human CASP8
View immunogen

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Purification

Antigen affinity chromatography, Protein A

Storage buffer

PBS, pH 7.4

Contains

0.09% sodium azide

Storage conditions

Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.

Shipping conditions

Ambient (domestic); Wet ice (international)

RRID

AB_2068473

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; Fas-linked ICE-like protease; 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

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Gene Aliases: ALPS2B; CAP4; CASP-8; CASP8; FLICE; MACH; MCH5

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UniProt ID: (Human) Q14790, (Mouse) O89110

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Entrez Gene ID: (Human) 841, (Mouse) 12370

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Function(s)
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 endopeptidase activity hydrolase activity protein heterodimerization activity
Process(es)
angiogenesis neural tube formation proteolysis apoptotic process activation of cysteine-type endopeptidase activity involved in apoptotic process heart development extrinsic apoptotic signaling pathway via death domain receptors macrophage differentiation response to tumor necrosis factor TRAIL-activated apoptotic signaling pathway regulation of apoptotic process 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 cardiac muscle tissue development protein heterooligomerization proteolysis involved in cellular protein catabolic process negative regulation of necroptotic process regulation of thymocyte apoptotic process apoptotic signaling pathway extrinsic apoptotic signaling pathway execution phase of apoptosis activation of cysteine-type endopeptidase activity hepatocyte apoptotic process regulation of apoptotic signaling pathway positive regulation of extrinsic apoptotic signaling pathway 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 response to cobalt ion response to estradiol response to lipopolysaccharide TRIF-dependent toll-like receptor signaling pathway suppression by virus of host cysteine-type endopeptidase activity involved in apoptotic process T cell activation B cell activation response to antibiotic 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 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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