TrimTAC1

TrimTAC1 (24 h) potently degrades BRD4 in PANC-1 cells, with a DC₅₀ of 0.649 nM and a maximum degradation rate of 71%^[1].
TrimTAC1 (3 days) inhibits the proliferation of PANC-1 cells, with a GI₅₀ value of 0.103 μM^[1].
TrimTAC1 forms a highly stable, low-energy conformation with BRD4. The spatial orientation of this conformation facilitates efficient ubiquitination, which correlates with its experimentally observed high activity in degrading BRD4 within the TRIM21-TrimTAC1-BRD4 ternary complex^[1].
TrimTAC1 exhibits high thermodynamic stability and shows strong positive cooperative binding between TRIM21 and BRD4. The interactions in the TRIM21-TrimTAC1-BRD4 ternary complex are mediated by key hydrophobic and electrostatic residues^[1].
TrimTAC1 exhibits physicochemical properties consistent with the favorable membrane permeability and solubility required for targeted protein degrader applications (log P = 4.7, log D_7.4 = 4.9)^[1].
TrimTAC1 (0-20 μM; 12 h) exhibits no molecular glue degrader activity against nucleoporins in IFNγ-pretreated A549 cells^[2].
TrimTAC1 (4 h) does not degrade monomeric mEGFP-BRD4^BD2 in A549 cells expressing TRIM21^D355A[2].
TrimTAC1 (2 μM; 4 h) efficiently degrades condensate-forming NUP98^FG-mEGFP-BRD4^BD2 in A549 cells expressing TRIM21^D355A via a proteasome- and ubiquitination-dependent mechanism^[2].
TrimTAC1 (2 μM; 4 h) selectively degrades mEGFP fusion proteins that form condensates (PML, coilin, NPM1) in A549 cells expressing TRIM21^D355A, but does not degrade non-condensate-forming mEGFP fusion proteins (CDK4, BTK)^[2].
TrimTAC1 (2 μM; 6 h) selectively degrades DNA-induced BRD4^BD2-mEGFP-cGAS condensates in HaCaT cells expressing TRIM21^D355A, without affecting soluble BRD4^BD2-mEGFP-cGAS^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.