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loss of ASC driven tumor development is counterbalanced in the identical cell by the inhibition of pro-tumorigenic inflammation in the tumor cell itself
the deubiquitinating enzyme USP50 binds to the ASC protein and subsequently regulates the inflammasome signaling pathway.
ASC self-associates and binds NLRP3 (show NLRP3 ELISA Kits) PYD through equivalent protein regions, with higher binding affinity for the latter. These regions are located at opposite sides of the protein allowing multimeric complex formation previously shown in ASC PYD fibril assemblies.
Our data identify RIPK3 (show RIPK3 ELISA Kits) and the ASC inflammasome as key tumor suppressors in AML (show RUNX1 ELISA Kits).
The role of the danger signals ASC and HMGB1 (show HMGB1 ELISA Kits) in the Fusobacterium nucleatum infection of gingival epithelial cells.
Data show that NOD-like receptor signaling genes NOD2 (show NOD2 ELISA Kits), PYCARD, CARD6 (show CARD6 ELISA Kits), and IFI16 (show IFI16 ELISA Kits) are upregulated in psoriatic epidermis.
The methylated status of ASC/TMS1 promoter had the potential applicability for clinical evaluation the prognosis of gastric cancer
it appears that ASC transcript expression may be a surrogate marker for depression and may represent a link between depression and the altered immune responses observed in these categories of individuals with elevated depressive symptoms.
The proteins of NLRP3 (show NLRP3 ELISA Kits), ASC, and caspase-1 (show CASP1 ELISA Kits) 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.
Our data identify RIPK3 (show RIPK3 ELISA Kits) and the ASC (show STS ELISA Kits) inflammasome as key tumor suppressors in AML (show RUNX1 ELISA Kits).
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
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