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The protein encoded by CARD9 is a member of the CARD protein family, which is defined by the presence of a characteristic caspase-associated recruitment domain (CARD). Additionally we are shipping CARD9 Antibodies (73) and CARD9 Kits (1) and many more products for this protein.
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CARD9 knockout alleviated HFD-induced insulin (show INS Proteins) resistance and glucose intolerance, prevented myocardial dysfunction with preserved cardiac fractional shortening and cardiomyocyte contractile properties. CARD9 knockout also significantly decreased the number of infiltrated macrophages in the heart with reduced myocardium-, plasma-, and macrophage-derived cytokines
a possible role for the Syk (show SYK Proteins)-CARD9 pathway in DCs in excessive inflammation of IFV-infected lungs.
CARD9 mediates necrotic smooth muscle cell-induced inflammation in macrophages contributing to neointima formation of vein grafts.
Mincle (show CLEC4E Proteins) Activation and the Syk (show SYK Proteins)/Card9 Signaling Axis Are Central to the Development of Autoimmune Disease of the Eye
CARD9 reduces viability specifically in males and promotes tumorigenesis specifically in the large intestines of these male mice.
Ubiquitination of CARD9 by TRIM62 regulates CARD9-mediated anti-fungal immunity.
CARD9-dependent production of TNF-alpha (show TNF Proteins) enhances the candidacidal capacity of neutrophils, limiting fungal disease during disseminated C. tropicalis infection.
Results indicating that CARD9 is a regulator of metastasis-associated macrophages will lead to new insights into evolution of the microenvironments supporting tumor metastasis.
Rapid CD4 (show CD4 Proteins)+ T-cell responses to bacterial flagellin (show FliC Proteins) require dendritic cell expression of Syk (show SYK Proteins) and CARD9.
CARD9 regulates H-Ras (show HRAS Proteins) activation by linking Ras-GRF1 (show RASGRF1 Proteins) to H-Ras (show HRAS Proteins), which mediates Dectin-1 (show CLEC7A Proteins)-induced extracellular signal-regulated protein kinase (show CDK7 Proteins) (ERK (show EPHB2 Proteins)) activation and proinflammatory responses when stimulated by their ligands.
Card9 in severe acute pancreatitis patients was overexpressed, suggesting the close correlation with the outcome and severity of pancreatic injury in patients.
CARD9 allele C (p = 0.012) and genotype CC (p = 0.012) were significant protective factors against ankylosing spondylitis only in HLA-B27-negative patients.
The findings linked, for the first time, mutations leading to CARD9 deficiencies with susceptibility to opportunistic filamentous fungi.
Chronic and invasive fungal infections have been described in a Turkish consanguineous family with CARD9 deficiency.
We observed no significant association between the investigated CARD9 SNPs and the susceptibility of either Crohn's disease or ulcerative colitis
This study identified two novel independent loci (MAP3K14 (show MAP3K14 Proteins) and CARD9) strongly associated with joint damage in Mexican Americans and European Americans and a few shared loci showing suggestive evidence for association.
Impaired RASGRF1 (show RASGRF1 Proteins)/ERK (show EPHB2 Proteins)-mediated GM-CSF (show CSF2 Proteins) response characterizes CARD9 deficiency in French-Canadians.
our data highlight the critical role of CARD9-dependent neutrophil trafficking into the central nervous system
A CARD9 variant (protective against inflammatory bowel disease)is C-terminally truncated and acts in a dominant-negative manner for CARD9-mediated cytokine production. K125 is the CARD9 ubiquitinated residue. Ubiquitination is needed for CARD9 activity.
These results indicate that CARD9 is indispensable for Phialophora verrucosa killing by polymorphonuclear neutrophils.
The protein encoded by this gene is a member of the CARD protein family, which is defined by the presence of a characteristic caspase-associated recruitment domain (CARD). CARD is a protein interaction domain known to participate in activation or suppression of CARD containing members of the caspase family, and thus plays an important regulatory role in cell apoptosis. This protein was identified by its selective association with the CARD domain of BCL10, a postive regulator of apoptosis and NF-kappaB activation, and is thought to function as a molecular scaffold for the assembly of a BCL10 signaling complex that activates NF-kappaB. Several alternatively spliced transcript variants have been observed, but their full-length nature is not clearly defined.
caspase recruitment domain-containing protein 9
, Caspase recruitment domain-containing protein 9
, caspase recruitment domain family, member 9
, caspase recruitment domain protein 9
, caspase recruitment domain-containing protein 9-like