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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 (106) and PYCARD Proteins (8) and many more products for this protein.
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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 ELISA Kits) and caspase-1 (show CASP1 ELISA Kits) via different domains.
The proteins (HSP90b (show HSP90AB1 ELISA Kits), TSM1 and L-plastin (show LCP1 ELISA Kits)) in the current study may hold potential in differentiating between melanoma and benign nevi in diagnostically challenging cases.
caspase-1 (show CASP1 ELISA Kits)/ASC inflammasomes play a significant role in the activation of IL-1beta (show IL1B ELISA Kits)/ROS (show ROS1 ELISA Kits) and NF-kappaB (show NFKB1 ELISA Kits) 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 ELISA Kits)(NLRP3, PYCARD) in obesity-induced adipose inflammation.
Data indicate that apoptosis-associated speck-like protein containing a caspase (show CASP3 ELISA Kits) 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
ASC PYD prevented complex formation with NALP3 (show NLRP3 ELISA Kits) PYD in vitro
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 ELISA Kits)) plays a pro-inflammatory/pathogenic role in the onset of antigen-induced arthritis (AIA) through apoptosis-associated speck-like Pycard protein (ASC (show STS ELISA Kits))-dependent stimulation of interleukin-1 beta (IL-1beta (show IL1B ELISA Kits)) production.
report herein that lack of ASC (show STS ELISA Kits) does not confer preferential protection in response to P. aeruginosa acute infection and that ASC (show STS ELISA Kits)(-/-) mice are capable of producing robust amounts of IL-1beta (show IL1B ELISA Kits) comparable with C57BL/6 mice
These data identify a novel non-canonical immunoregulatory function of NLRP3 (show NLRP3 ELISA Kits) and ASC (show STS ELISA Kits) in autoimmunity.
a significant role for NLRP3 (show NLRP3 ELISA Kits) and ASC (show STS ELISA Kits) in prion (show PRNP ELISA Kits) pathogenesis
ASC (show STS ELISA Kits)-driven caspase-1 (show CASP1 ELISA Kits) autoprocessing and speck formation are dispensable for the activation of caspase-1 (show CASP1 ELISA Kits) and the NLRP1b inflammasome.
IKKalpha (show CHUK ELISA Kits) controls the inflammasome at the level of the adaptor molecule ASC (show STS ELISA Kits), which interacts with IKKalpha (show CHUK ELISA Kits) in the nucleus of resting macrophages in an IKKalpha (show CHUK ELISA Kits) kinase-dependent manner.
Hypoxia-induced elevated right ventricular pressure and remodeling were attenuated in mice lacking the inflammasome adaptor protein ASC (show STS ELISA Kits), suggesting that inflammasomes play an important role in the pathogenesis of pulmonary hypertension.
gene deficiency results in absence of IL-1beta (show IL1B ELISA Kits) 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