| Cat. # | Size | Qty. | Price |
|---|---|---|---|
| 72032T | 1 Kit (6 x 20 microliters) |
|
| Product Includes | Quantity | Applications | Reactivity | MW(kDa) | Isotype |
|---|---|---|---|---|---|
| CRBN (D8H3S) Rabbit mAb 71810 | 20 µl |
|
H M R | 55 | Rabbit IgG |
| CUL4A Antibody 2699 | 20 µl |
|
H Mk | 80, 82 | Rabbit |
| DDB-1 (D4C8) Rabbit mAb 6998 | 20 µl |
|
H M R Mk | 127 | Rabbit IgG |
| RBX1 (D3J5I) Rabbit mAb 11922 | 20 µl |
|
H M R Mk | 13 | Rabbit IgG |
| NEDD8 (19E3) Rabbit mAb 2754 | 20 µl |
|
H M R Mk | 9 | Rabbit IgG |
| Ubiquitin (E4I2J) Rabbit mAb 43124 | 20 µl |
|
All | Rabbit IgG | |
| Anti-rabbit IgG, HRP-linked Antibody 7074 | 100 µl |
|
Goat |
Product Information
Monoclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to residues surrounding Pro44 of human CRBN protein, Gly832 of human DDB-1 protein, Gly35 of human ubiquitin protein, the amino terminus of human NEDD8 protein, and the carboxy terminus of human RBX1 protein. Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser12 of human CUL4A. Antibodies are purified by peptide affinity chromatography.
Targeted protein degradation is an experimental method of drug-based protein targeting that leverages endogenous E3 ubiquitin ligases and the ubiquitin proteasome system (UPS) to selectively degrade target proteins. It is being actively explored as a therapeutic strategy to target and degrade specific proteins that contribute to disease progression (1). This approach differs from traditional small-molecule therapeutics that seek to suppress disease proteins (e.g., kinases) by sterically blocking catalytic domains. Protein-targeting chimeras (PROTACs) are the prototypical protein "degraders”. PROTACs are bivalent chemical ligands that induce proximity between a target protein and an E3 ubiquitin ligase, resulting in ubiquitination of the target protein, and its subsequent degradation by the UPS (2,3). Cereblon (CRBN) is the substrate-recognition component of a Cullin-RING-ubiquitin ligase complex (CRL4/CRBN) that was among the first to be recognized for its therapeutic potential via targeted protein degradation (4). The CRL4/CRBN complex is comprised of CRBN, DDB-1, RBX1, and the scaffold protein CUL4A; its ligase activity is dynamically regulated via the covalent modification (neddylation) of CUL4A by NEDD8 (5). In unrelated mechanistic studies of multiple myeloma drugs, it was revealed that phthalimides (e.g., thalidomide, lenalidomide) promoted CRBN-dependent recruitment, ubiquitination, and proteasomal degradation of the immunological transcription factors Ikaros (IKZF1) and Aiolos (IKZF3) (6). The discovery that phthalimides were functioning as PROTACs, by eliciting the selective degradation of what were previously considered "undruggable" protein targets, led to a rapid acceleration and expansion of research into targeted protein degradation, with the promise of novel therapies for diseases deemed largely intractable using conventional small-molecule therapies (7-9).
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STRING - Known and Predicted Protein-Protein Interactions.
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