Cell penetrant Proteolysis Targeting Chimera (PROTAC) compound based on (+)-JQ1 (Cat.No. 4499) conjugated to a von Hippel-Lindau (VHL) ligand. Rationally designed based on a ternary complex crystal structure to improve selectivity for BRD4 degradation compared to MZ1 (Cat.No. 6154). Demonstrates profound and selective degradation of BRD4 in cells at 1-3 μM, with negligible loss of BRD2 and BRD3.
PROTACs are bi-functional small molecules that harness the ubiquitin/proteasome system (UPS) to selectively and catalytically remove target proteins from cells.
Sold under licence from the University of Dundee
|Storage||Store at -20°C|
The technical data provided above is for guidance only. For batch specific data refer to the Certificate of Analysis.
All Tocris products are intended for laboratory research use only.
|Solvent||Max Conc. mg/mL||Max Conc. mM|
Preparing Stock Solutions
The following data is based on the product molecular weight 972.68. Batch specific molecular weights may vary from batch to batch due to solvent of hydration, which will affect the solvent volumes required to prepare stock solutions.
|Concentration / Solvent Volume / Mass||1 mg||5 mg||10 mg|
|1 mM||1.03 mL||5.14 mL||10.28 mL|
|5 mM||0.21 mL||1.03 mL||2.06 mL|
|10 mM||0.1 mL||0.51 mL||1.03 mL|
|50 mM||0.02 mL||0.1 mL||0.21 mL|
References are publications that support the products' biological activity.
Gadd (2017) Structural basis of PROTAC cooperative recognition for selective protein degradation. Nat.Chem.Biol. 13 514 PMID: 28288108
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Keywords: AT 1, supplier, PROTAC, Proteolysis, targeted, chimeras, Bromodomain, BRD2, BRD3, BRD4, BET, proteins, JQ1, VHL, E3, ubiquitin, ligase, AT1, Ubiquitin, E3, Ligases, PROTACs, Bromodomains, Ubiquitin, E3, Ligases, Tocris Bioscience
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Programmed Cell Death Poster
There are two currently recognized forms of programmed cell death: apoptosis and necroptosis. This poster summarizes the signaling pathways involved in apoptosis, necroptosis and cell survival following death receptor activation, and highlights the influence of the molecular switch, cFLIP, on cell fate.