CAND1 (D1F2) Rabbit mAb #8759
- WB
- IP
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 130 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Protocol
Specificity / Sensitivity
CAND1 (D1F2) Rabbit mAb recognizes endogenous levels of total CAND1 protein. Based upon sequence alignment, this antibody is not predicted to cross-react with CAND2/TIP120B.
Species Reactivity:
Human, Mouse, Rat, Monkey
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Chicken, Dog, Pig, Guinea Pig
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala561 of human CAND1 protein.
Background
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).
- Liu, J. et al. (2002) Mol Cell 10, 1511-8.
- Zheng, J. et al. (2002) Mol Cell 10, 1519-26.
- Min, K.W. et al. (2003) J Biol Chem 278, 15905-10.
- Goldenberg, S.J. et al. (2004) Cell 119, 517-28.
- Wee, S. et al. (2005) Nat Cell Biol 7, 387-91.
- Wu, J.T. et al. (2005) Nat Cell Biol 7, 1014-20.
- Cope, G.A. and Deshaies, R.J. (2006) BMC Biochem 7, 1.
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