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PYCARD encodes an adaptor protein that is composed of two protein-protein interaction domains: a N-terminal PYRIN-PAAD-DAPIN domain (PYD) and a C-terminal caspase-recruitment domain (CARD). Additionally we are shipping PYCARD Antibodies (144) and PYCARD Kits (9) and many more products for this protein.
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The proteins of NLRP3 (show NLRP3 Proteins), ASC, and caspase-1 (show CASP1 Proteins) were observed in infiltrating inflammatory cells in cholesteatoma and chronic otitis media.
ASC/TMS1 methylation was significantly correlated with higher tumor nuclear grade. ASC/TMS1 is a novel functional tumor suppressor in renal carcinogenesis.
ASC Induces Procaspase-8 Death Effector Domain Filaments
ASC interacts with NALP3 (show NLRP3 Proteins) and caspase-1 (show CASP1 Proteins) via different domains.
The proteins (HSP90b (show HSP90AB1 Proteins), TSM1 and L-plastin (show LCP1 Proteins)) in the current study may hold potential in differentiating between melanoma and benign nevi in diagnostically challenging cases.
caspase-1 (show CASP1 Proteins)/ASC inflammasomes play a significant role in the activation of IL-1beta (show IL1B Proteins)/ROS (show ROS1 Proteins) and NF-kappaB (show NFKB1 Proteins) signaling of cytokine gene expression for T. cruzi control in human and mouse macrophages.
Neutralization of ASC improves sperm motility in men with spinal cord injuries.
Transcriptome analysis of human adipocytes implicates the NOD-like receptor pathway (show NLRP3 Proteins)(NLRP3, PYCARD) in obesity-induced adipose inflammation.
Data indicate that apoptosis-associated speck-like protein containing a caspase (show CASP3 Proteins) recruitment domain (ASC) is highly expressed in medulloblastomas.
R42W mutation had a significant effect on structure and increased stability. Although the R42W mutant exhibited reduced interaction with ASC
Data show that T cell-intrinsic PYD and CARD domain containing protein ASC is required for TH17-mediated experimental autoimmune encephalomyelitis (EAE).
Data suggest that interleukin 22 (IL-22 (show IL22 Proteins)) plays a pro-inflammatory/pathogenic role in the onset of antigen-induced arthritis (AIA) through apoptosis-associated speck-like Pycard protein (ASC (show STS Proteins))-dependent stimulation of interleukin-1 beta (IL-1beta (show IL1B Proteins)) production.
report herein that lack of ASC (show STS Proteins) does not confer preferential protection in response to P. aeruginosa acute infection and that ASC (show STS Proteins)(-/-) mice are capable of producing robust amounts of IL-1beta (show IL1B Proteins) comparable with C57BL/6 mice
These data identify a novel non-canonical immunoregulatory function of NLRP3 (show NLRP3 Proteins) and ASC (show STS Proteins) in autoimmunity.
a significant role for NLRP3 (show NLRP3 Proteins) and ASC (show STS Proteins) in prion (show PRNP Proteins) pathogenesis
ASC (show STS Proteins)-driven caspase-1 (show CASP1 Proteins) autoprocessing and speck formation are dispensable for the activation of caspase-1 (show CASP1 Proteins) and the NLRP1b inflammasome.
IKKalpha (show CHUK Proteins) controls the inflammasome at the level of the adaptor molecule ASC (show STS Proteins), which interacts with IKKalpha (show CHUK Proteins) in the nucleus of resting macrophages in an IKKalpha (show CHUK Proteins) kinase-dependent manner.
Hypoxia-induced elevated right ventricular pressure and remodeling were attenuated in mice lacking the inflammasome adaptor protein ASC (show STS Proteins), suggesting that inflammasomes play an important role in the pathogenesis of pulmonary hypertension.
gene deficiency results in absence of IL-1beta (show IL1B Proteins) maturation in the middle ear response to non-typeable Haemophilus influenza, and in reduction of both leukocyte infiltration and macrophage phagocytosis
Data (including data from studies using knockout mice) suggest that Asc is required for macrophage activation and inflammasome-dependent secretion of interleukin 1beta from peritoneal macrophages upon exposure to silica particles.
This gene encodes an adaptor protein that is composed of two protein-protein interaction domains: a N-terminal PYRIN-PAAD-DAPIN domain (PYD) and a C-terminal caspase-recruitment domain (CARD). The PYD and CARD domains are members of the six-helix bundle death domain-fold superfamily that mediates assembly of large signaling complexes in the inflammatory and apoptotic signaling pathways via the activation of caspase. In normal cells, this protein is localized to the cytoplasm\; however, in cells undergoing apoptosis, it forms ball-like aggregates near the nuclear periphery. Two transcript variants encoding different isoforms have been found for this gene.
apoptosis-associated speck-like protein containing a CARD
, caspase recruitment domain-containing protein 5
, target of methylation-induced silencing 1
, PYD and CARD domain-containing protein