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Product Details
MA5-15914
Applications
Tested Dilution
Publications
Product Specifications
Species Reactivity
Human,
Mouse,
Non-human primate,
Rat
Published species
Rat
Host/Isotype
Mouse
/ IgG1
Class
Monoclonal
Type
Antibody
Clone
1H11
Immunogen
Purified recombinant fragment of human CASP8 expressed in E. Coli.
Conjugate
Form
Liquid
Concentration
Conc. Not Determined
Storage buffer
ascites
Contains
0.03% sodium azide
Storage conditions
Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.
Shipping conditions
Wet ice
RRID
AB_11157670
Product Specific Information
MA5-15914 targets CASP8 in indirect ELISA, FACS, IHC, and WB applications and shows reactivity with Human, mouse, Non-human primate, and Rat samples.
The MA5-15914 immunogen is purified recombinant fragment of human CASP8 expressed in E. Coli. .
MA5-15914 detects CASP8 which has a predicted molecular weight of approximately 26kDa.
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.
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
Gene Aliases: ALPS2B; CAP4; CASP-8; CASP8; FLICE; MACH; MCH5
UniProt ID: (Human) Q14790, (Rat) Q9JHX4, (Mouse) O89110
Entrez Gene ID: (Human) 841, (Rat) 64044, (Mouse) 12370
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
protein heterodimerization activity
hydrolase activity
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
angiogenesis
neural tube formation
heart development
extrinsic apoptotic signaling pathway via death domain receptors
negative regulation of necroptotic process
regulation of thymocyte apoptotic process
hepatocyte apoptotic process
regulation of apoptotic signaling pathway
positive regulation of extrinsic apoptotic signaling pathway
regulation of apoptotic process
cardiac muscle tissue development
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