Anti-CAND1 polyclonal antibody (CABT-BL6317)


Host Species
Antibody Isotype
Species Reactivity
human CAND1 (residues 5-245) [GST-tagged]


Application Notes
WB: 1ug/ml
IP: use 2ug/mg of cell extract
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.


Alternative Names
CAND1; cullin-associated and neddylation-dissociated 1; TIP120; TIP120A; cullin-associated NEDD8-dissociated protein 1; p120 CAND1
Entrez Gene ID
UniProt ID


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Cand1 Promotes Assembly of New SCF Complexes through Dynamic Exchange of F Box Proteins


Authors: Pierce, Nathan W.; Lee, J. Eugene; Liu, Xing; Sweredoski, Michael J.; Graham, Robert L. J.; Larimore, Elizabeth A.; Rome, Michael; Zheng, Ning; Clurman, Bruce E.; Hess, Sonja; Shan, Shu-ou; Deshaies, Raymond J.

The modular SCF (Skp1, cullin, and F box) ubiquitin ligases feature a large family of F box protein substrate receptors that enable recognition of diverse targets. However, how the repertoire of SCF complexes is sustained remains unclear. Real-time measurements of formation and disassembly indicate that SCFFbxw7 is extraordinarily stable, but, in the Nedd8-deconjugated state, the cullin-binding protein Cand1 augments its dissociation by one-million-fold. Binding and ubiquitylation assays show that Cand1 is a protein exchange factor that accelerates the rate at which Cul1-Rbx1 equilibrates with multiple F box protein-Skp1 modules. Depletion of Cand1 from cells impedes recruitment of new F box proteins to pre-existing Cul1 and profoundly alters the cellular landscape of SCF complexes. We suggest that catalyzed protein exchange may be a general feature of dynamic macromolecular machines and propose a hypothesis for how substrates, Nedd8, and Cand1 collaborate to regulate the cellular repertoire of SCF complexes.

PIKES Analysis Reveals Response to Degraders and Key Regulatory Mechanisms of the CRL4 Network


Authors: Reichermeier, Kurt M.; Straube, Ronny; Reitsma, Justin M.; Sweredoski, Michael J.; Rose, Christopher M.; Moradian, Annie; den Besten, Willem; Hinkle, Trent; Verschueren, Erik; Petzold, Georg; Thomae, Nicolas H.; Wertz, Ingrid E.; Deshaies, Raymond J.; Kirkpatrick, Donald S.

Co-opting Cullin4 RING ubiquitin ligases (CRL4s) to inducibly degrade pathogenic proteins is emerging as a promising therapeutic strategy. Despite intense efforts to rationally design degrader molecules that co-opt CRL4s, much about the organization and regulation of these ligases remains elusive. Here, we establish protein interaction kinetics and estimation of stoichiometries (PIKES) analysis, a systematic proteomic profiling platform that integrates cellular engineering, affinity purification, chemical stabilization, and quantitative mass spectrometry to investigate the dynamics of interchangeable multiprotein complexes. Using PIKES, we show that ligase assemblies of Cullin4 with individual substrate receptors differ in abundance by up to 200-fold and that Cand1/2 act as substrate receptor exchange factors. Furthermore, degrader molecules can induce the assembly of their cognate CRL4, and higher expression of the associated substrate receptor enhances degrader potency. Beyond the CRL4 network, we show how PIKES can reveal systems level biochemistry for cellular protein networks important to drug development.

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