CARDs (caspase recruitment domain) are homotypic protein-protein interaction motifs belonging to the death domain (DD)-fold superfamily. Homotypic interactions among CARD-containing proteins can occur with various proteins, including the inactive zymogen forms of caspases which have N-terminal pro-domains containing complementary CARDs. These interactions can result in the formation of multiprotein complexes, leading to protease cleavage and caspase activation. Most proteins containing a CARD are involved in signal transduction pathways that regulate apoptosis, adaptive immunity, or innate immunity including NF-kB activation and inflammation. There is a large number of CARD containing proteins, and the unique function of each remains to be fully elucidated. CARD6 is a CARD-containing protein with a domain structure that doesn't appear to be shared by any other protein. CARD6 has been found to associate with microtubules, and is structurally and potentially functionally related to the superfamily of interferon (INF)-inducible GTPases. INF-inducible GTPases belong to a growing family of host defense proteins that confer cell immunity. Specifically, is thought that CARD6 may act as a pattern recognition receptor that combats pathogens in a cell-autonomous manner. CARD6 is a 1037aa protein, and CINCIN1 is 311aa splice variant of CARD6.
Applications:
Suitable for use in Western Blot, Immunohistochemistry and Immunoprecipitation. Other applications not tested.
Recommended Dilution:
Western Blot: 1:1000-1:2000
Immunohistochemistry (formalin fixed paraffin embedded): 1:1000-1:5000
Immunoprecipitation: 1:50-1:200
Immunohistochemistry: Frozen
Optimal dilutions to be determined by the researcher.
Positive Control:
CNS, lymphatic tissues
Storage and Stability:
May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.