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Invitrogen

Caspase 8 p18 Polyclonal Antibody

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Caspase 8 p18 Polyclonal Antibody

Product Details

PA5-95047

Applications
Tested Dilution
Publications

Western Blot (WB)

0.1-0.5 µg/mL
-

Immunohistochemistry (Paraffin) (IHC (P))

0.5-1 µg/mL
-
Product Specifications

Species Reactivity

Human

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

A synthetic peptide corresponding to a sequence at the N-terminus of human Caspase-8 (p18) (257-277aa NNHNFAKAREKVPKLHSIRDR).
3D Epitope / Immunogen

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Lyophilized

Concentration

500 µg/mL

Amount

100 µg

Purification

Affinity chromatography

Storage buffer

PBS with 5mg BSA

Contains

0.05mg sodium azide, 0.05mg thimerosal

Storage conditions

-20°C

Shipping conditions

Ambient (domestic); Wet ice (international)

RRID

AB_2806853

Product Specific Information

Reconstitute with 0.2 mL of distilled water to yield a concentration of 500 µg/mL.

Positive Control - WB: A549 whole cell, HELA whole cell. IHC: Human Tonsil Tissue.|Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.

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.

⚠WARNING: This product can expose you to chemicals including mercury, which is known to the State of California to cause birth defects or other reproductive harm. For more information go to www.P65Warnings.ca.gov.

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; caspase 8, apoptosis-related cysteine peptidase; caspase 8, apoptosis-related cysteine protease; caspase precursor; caspase-8s; 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

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Gene Aliases: ALPS2B; CAP4; Casp-8; FLICE; MACH; MCH5

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UniProt ID: (Human) Q14790

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Entrez Gene ID: (Human) 841

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Function(s)
endopeptidase activity cysteine-type endopeptidase activity death receptor binding protein binding peptidase activity cysteine-type peptidase activity cysteine-type endopeptidase activator activity involved in apoptotic process ubiquitin protein ligase binding death effector domain binding identical protein binding macromolecular complex binding scaffold protein binding
Process(es)
angiogenesis regulation of cytokine production regulation of immune system process proteolysis apoptotic process heart development extrinsic apoptotic signaling pathway via death domain receptors positive regulation of signal transduction regulation of tumor necrosis factor-mediated signaling pathway protein processing natural killer cell activation cell differentiation protein catabolic process macrophage differentiation positive regulation of cell migration response to cobalt ion response to estradiol response to lipopolysaccharide positive regulation of interleukin-1 beta production response to tumor necrosis factor TRAIL-activated apoptotic signaling pathway T cell activation B cell activation regulation of apoptotic process chordate embryonic development positive regulation of apoptotic process positive regulation of I-kappaB kinase/NF-kappaB signaling negative regulation of I-kappaB kinase/NF-kappaB signaling positive regulation of neuron apoptotic process regulation of innate immune response response to ethanol positive regulation of macrophage differentiation positive regulation of proteolysis animal organ development protein maturation negative regulation of necroptotic process syncytiotrophoblast cell differentiation involved in labyrinthine layer development pyroptosis cellular response to mechanical stimulus death-inducing signaling complex assembly response to anesthetic apoptotic signaling pathway extrinsic apoptotic signaling pathway execution phase of apoptosis self proteolysis positive regulation of execution phase of apoptosis
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