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The antibody against CARD8 was raised in rabbit using the Recombinant Human Caspase recruitment domain-containing protein 8 protein (1-200AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, IHC.
The antibody against CARD8 was raised in rabbit using the Recombinant Human Caspase recruitment domain-containing protein 8 protein (1-200AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, IHC.
$299.00
| Cat.No | ADC-45171A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | CARD8 |
| Form | Liquid | Species Reactivity | Human |
| Isotype | IgG | Storage Buffer | 50% Glycerol, PBS with 0.02% sodium azide, pH7.3. |
| Purification Method | Antigen affinity purified | Conjugate | Non-conjugated |
| Application | ELISA, IHC | Storage | Upon receipt |
| Immunogen Description | Recombinant Human Caspase recruitment domain-containing protein 8 protein (1-200AA) | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | Q9Y2G2 |
Uniprot Id
Q9Y2G2
Target Species
Human
Target Name
CARD8
Target Full Name
Caspase recruitment domain-containing protein 8
Target Function
Inflammasome sensor, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis of CD4(+) T-cells and macrophages. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as HIV-1 protease activity or Val-boroPro inhibitor, and mediates CARD8 inflammasome activation. In response to pathogen-associated signals, the N-terminal part of CARD8 is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (Caspase recruitment domain-containing protein 8, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the CARD8 inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis. Ability to sense HIV-1 protease activity leads to the clearance of latent HIV-1 in patient CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade CARD8-sensing when its protease remains inactive in infected cells prior to viral budding. Also acts as a negative regulator of the NLRP3 inflammasome. May also act as an inhibitor of NF-kappa-B activation.; Constitutes the precusor of the CARD8 inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals.; Regulatory part that prevents formation of the CARD8 inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of CARD8 (Caspase recruitment domain-containing protein 8, C-terminus), preventing activation of the CARD8 inflammasome. In response to pathogen-associated signals, this part is ubiquitinated by the N-end rule pathway and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the CARD8 inflammasome (Probable).; Constitutes the active part of the CARD8 inflammasome. In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of CARD8 (Caspase recruitment domain-containing protein 8, N-terminus), preventing activation of the CARD8 inflammasome. In response to pathogen-associated signals, the N-terminal part of CARD8 is degraded by the proteasome, releasing this form, which polymerizes to form the CARD8 inflammasome complex: the CARD8 inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis.
Target Subcellular Location
Cytoplasm. Nucleus.; [Caspase recruitment domain-containing protein 8, C-terminus]: Inflammasome.
Target Tissue Specificity
High expression in lung, ovary, testis and placenta. Lower expression in heart, kidney and liver. Also expressed in spleen, lymph node and bone marrow.
Target Synonyms
Apoptotic protein NDPP 1; Apoptotic protein NDPP1; CARD 8; CARD inhibitor of NF kappa B activating ligand; CARD inhibitor of NF kappaB activating ligand; CARD inhibitor of NF kappaB activating ligands; CARD-inhibitor of NF-kappa-B-activating ligand; CARD8; CARD8_HUMAN; CARDINAL; Caspase recruitment domain containing protein 8; Caspase recruitment domain family member 8; Caspase recruitment domain protein 8; Caspase recruitment domain-containing protein 8; DACAR; Dakar; DKFZp779L0366; FLJ18119; FLJ18121; KIAA0955; MGC57162; NDPP 1; NDPP; NDPP1; TUCAN; Tumor up regulated CARD containing antagonist of CASP9; Tumor up regulated CARD containing antagonist of caspase 9; Tumor up-regulated CARD-containing antagonist of CASP9; tumor up-regulated CARD-containing antagonist of caspase nine; Tumor upregulated CARD containing antagonist of CASP9
Target Background
The protein encoded by this gene belongs to the caspase recruitment domain (CARD)-containing family of proteins, which are involved in pathways leading to activation of caspases or nuclear factor kappa-B (NFKB). This protein may be a component of the inflammasome, a protein complex that plays a role in the activation of proinflammatory caspases. It is thought that this protein acts as an adaptor molecule that negatively regulates NFKB activation, CASP1-dependent IL1B secretion, and apoptosis. Polymorphisms in this gene may be associated with a susceptibility to rheumatoid arthritis. Alternatively spliced transcript variants have been described for this gene.
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