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Human PYCARD Protein expressed in Wheat germ - ABIN1316968
Shi, Wang, Li, Zhan, Tang, Fina, Su, Pratt, Bu, Hildebrand, Lyon, Scott, Quan, Sun, Russell, Arnett, Jurek, Chen, Kravchenko, Mathison, Moresco, Monson, Ulevitch, Beutler: NLRP3 activation and mitosis are mutually exclusive events coordinated by NEK7, a new inflammasome component. in Nature immunology 2016
ASC CpG methylation may prove to be a primary regulator of the pathogenesis of chronic inflammatory diseases such as heart failure.
besides its role in the inhibition of the NF-kappaB (show NFKB1 Proteins) pathway, NLRC3 interferes with the assembly and activity of the NALP3 (show NLRP3 Proteins) inflammasome complex by competing with ASC for pro-caspase-1 (show CASP1 Proteins) binding
ASC Induces Apoptosis via Activation of Caspase-9 (show CASP9 Proteins) by Enhancing Gap Junction-Mediated Intercellular Communication.(
These data revealed that cross-linking of ASC(PYD) filaments via ASC(CARD) mediates the assembly of ASC foci.
Down-regulation of mRNA expression was found in cases in which CASP8 (show CASP8 Proteins), TMS1 (show SERINC3 Proteins) and DAPK (show DAPK1 Proteins) were hypermethylated.
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 (show USP50 Proteins) binds to the ASC protein and subsequently regulates the inflammasome signaling pathway.
ASC self-associates and binds NLRP3 (show NLRP3 Proteins) 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 Proteins) and the ASC inflammasome as key tumor suppressors in AML (show RUNX1 Proteins).
The role of the danger signals ASC and HMGB1 (show HMGB1 Proteins) in the Fusobacterium nucleatum infection of gingival epithelial cells.
Our cumulative findings indicate that ASC (show STS Proteins) suppresses cancer metastasis and progression via the modulation of cytoskeletal remodeling and the Src (show SRC Proteins)-caspase-8 (show CASP8 Proteins) signaling pathway.
these findings suggest that p205 (show GNB2L1 Proteins) controls expression of Asc (show STS Proteins) mRNA to regulate inflammasome responses. These findings expand on our understanding of immune-regulatory roles for the PYHIN protein family.
this study shows that ASC (show STS Proteins)-dependent Inflammasomes do not shape the commensal gut (show GUSB Proteins) microbiota composition
Our data identify RIPK3 (show RIPK3 Proteins) and the ASC (show STS Proteins) inflammasome as key tumor suppressors in AML (show RUNX1 Proteins).
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.
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