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Whole exome sequencing (WES) of an affected fetus, and subsequent Sanger sequencing of the second fetus, revealed a homozygous frameshift variant in CRADD, which encodes an adaptor protein that interacts with PIDD and caspase-2 to initiate apoptosis
The megalencephaly, lissencephaly variant, and intellectual disability associated with loss of CRADD/caspase-2-mediated apoptosis imply a role for CRADD/caspase-2 signaling in development of the human cerebral cortex.
The adaptor molecule RAIDD coordinates IKKepsilon and IRF7 interaction to ensure efficient expression of type I interferon.
define a novel function for CRADD in endothelial cells as an inducible suppressor of BCL10, a key mediator of responses to proinflammatory agonists
Crystals are trigonal and belong to space group P3(1)21 (or its enantiomorph P3(2)21) with unit-cell parameters a = 56.3, b = 56.3, c = 64.9 A and gamma = 120 degrees .
Study identified sequence variants in the known disease-causing genes SLC6A3 and FLVCR1, and present evidence to strongly support the pathogenicity of variants identified in TUBGCP6, BRAT1, SNIP1, CRADD, and HARS.
point mutations on RAIDD (R147E) and on PIDD (Y814A) exert a dominant negative effect on the formation of the PIDDosome, and that this effect cannot be applied after the PIDDosome has been formed
The expressions of PIDD and RAIDD are upregulated during tumour progression in renal cell carcinomas.
As a first step towards elucidating the molecular mechanisms of caspase-2 activation, data report the crystal structure of the RAIDD death domain at 2.0 A resolution.
PIDD death domain (DD) and RAIDD DD assemble into an oligomeric complex. Within the PIDDosome, the interaction between PIDD and RAIDD is mediated by a homotypic interaction between their death domains.
impaired expression of RAIDD in drug induced apoptosis may play a role in the multidrug resistance of osteosarcoma cells
The tumor-modulatory effects of Caspase-2 and Pidd1 do not require the scaffold protein Raidd
Neuronal caspase-2-dependent execution of neurons requires recptor-interacting protein RAIDD, not p53-inducible protein with a death domain (PIDD).
We show that CRADD interacts with BCL10 through its caspase recruitment domain and suppresses interactions between BCL10 and CARMA1
Overexpression of Raidd cDNA in 3T3L1 cells inhibited differentiation of the preadipocytes.
P53-induced protein with a death domain -induced apoptosis and growth suppression in embryonic fibroblasts depend on the adaptor protein receptor-interacting protein (RIP)-associated ICH-1/CED-3 homologous protein with a death domain (RAIDD).
The protein encoded by this gene is a death domain (CARD/DD)-containing protein and has been shown to induce cell apoptosis. Through its CARD domain, this protein interacts with, and thus recruits, caspase 2/ICH1 to the cell death signal transduction complex that includes tumor necrosis factor receptor 1 (TNFR1A), RIPK1/RIP kinase, and numbers of other CARD domain-containing proteins.
death domain-containing protein CRADD
, CASP2 and RIPK1 domain containing adaptor with death domain
, Death domain-containing protein CRADD
, death domain-containing protein cradd
, CASP2 and RIPK1 domain containing adaptor with death, gene 2
, RIP-associated ICH1/CED3-homologous protein with death domain
, RIP-associated protein with a death domain
, caspase and RIP adaptor with death domain
, death adaptor molecule RAIDD
, CASP2 and RIPK1 domain-containing adaptor with death domain
, caspase and RIP adapter with death domain