FKBP12 PROTAC dTAG-13

Target: dTAG-13 selectively targets FKBP12F36V fusion proteins for CRBN-mediated degradation.

Binding site: Its bumped FKBP ligand binds the engineered FKBP12F36V binding pocket.

Mechanism of action: FKBP12 PROTAC dTAG-13 is a CRBN-recruiting heterobifunctional degrader used in the dTAG system for rapid depletion of proteins fused to FKBP12F36V. The compound simultaneously engages the engineered FKBP12F36V tag and CRL4CRBN ubiquitin ligase machinery, inducing ubiquitination and proteasome-dependent degradation of the tagged protein of interest while sparing wild-type FKBP12. This tool is valuable for target validation, time-resolved functional studies, acute loss-of-protein experiments, and evaluation of immediate signaling or phenotypic consequences after selective degradation of genetically tagged targets.

• PROTAC-Mediated FKBP12 Degradation: FKBP12 PROTAC dTAG-13 is designed to facilitate the selective degradation of the FKBP12 protein through the ubiquitin-proteasome system. This application is crucial for studying protein function and interactions by enabling researchers to observe cellular consequences following targeted protein depletion.

• Targeted Protein Degradation in Signal Transduction: By employing FKBP12 PROTAC dTAG-13, researchers can investigate the role of FKBP12 in intracellular signaling pathways. This approach allows for precise modulation of protein levels, providing insights into the mechanistic underpinnings of signal transduction processes.

• Functional Genomics via PROTAC: Utilizing FKBP12 PROTAC dTAG-13, scientists can perform functional genomics studies by systematically degrading FKBP12, thereby elucidating its contribution to various cellular phenotypes. This application aids in identifying potential therapeutic targets by revealing the biological roles of specific proteins.

• PROTAC-Enabled Drug Discovery: FKBP12 PROTAC dTAG-13 serves as a powerful tool in drug discovery research, allowing for the examination of FKBP12 as a potential target. By observing the effects of its degradation, researchers can assess the viability of targeting this protein in therapeutic strategies.