Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
CAND1 Antibody recognizes endogenous levels of total CAND1 protein. This antibody may cross-react with CAND2.
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asn610 of human CAND1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Cullin-associated and neddylation-dissociated (CAND1)/TIP120A is a protein containing multiple HEAT repeats. It functions, in part, as an inhibitor of multiple cullin-RING ubiquitin ligases (CRLs) via binding to cullin-RBX complexes that are both unconjugated to NEDD8 and lack association with substrate recognition subunits (1-3). Indeed, CAND1 has been shown to bind all cullin family members in human cells and analysis of the crystal structure of human CAND1 bound to the CUL1-RBX1 complex suggests that CAND1 inhibits the activity of CRLs by sterically blocking both the substrate recognition subunit binding site and the NEDD8 conjugation site (1,3,4). Conversely, CAND1 binding to cullin-RBX complexes is incompatible with neddylation as NEDD8 conjugated to cullins blocks CAND1 binding, suggesting that CAND1 binds to cullins only after the COP9 signalosome has catalyzed cullin deneddylation. Through its ability to negatively regulate CRL assembly, CAND1 plays an integral part in facilitating CRL activation cycles that allow CRLs to utilize distinct substrate recognition subunits and protects these subunits from undergoing ubiquitin-dependent degradation (5-7).
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
Explore pathways related to this product.