CCT367766 formic is a third-generation cereblon-based protein degradation probe targeting pirin. Public product information describes it as a heterobifunctional protein degradation probe, also referred to as a PDP or PROTAC, that depletes pirin protein expression and binds both pirin and the CRBN-DDB1 complex. The pirin-recognition module provides target engagement, while the cereblon-directed module recruits CRL4-cereblon; the linker supports formation of a productive ternary complex suitable for ubiquitin transfer. Mechanistically, CCT367766 formic promotes pirin recruitment to cereblon-associated ubiquitination machinery and subsequent proteasome-dependent depletion. It is useful for studying pirin biology, chemical tractability of underexplored proteins, cereblon-based degrader design, target-engagement versus degradation relationships, and optimization of heterobifunctional probes for proteins with limited prior chemical biology tools. It should be interpreted through direct pirin-degradation and cereblon-dependency assays.
* For research and manufacturing use only. Not for human or clinical use.
| Size | Price | Stock | Quantity |
|---|---|---|---|
| -- | $-- | In stock |
Looking for different specifications? Click to request a custom quote!
Capabilities & Facilities
Popular Publications Citing BOC Sciences Products
Target: CCT367766 formic selectively targets pirin for cereblon-mediated proteasomal degradation.
Binding site: Its pirin ligand binds recombinant pirin while recruiting CRBN-DDB1 through cereblon.
Mechanism of action: CCT367766 formic is a third-generation, cereblon-based heterobifunctional protein degradation probe targeting pirin. It combines a pirin-binding ligand with a CRBN-recruiting moiety, enabling induced proximity between pirin and CRL4CRBN ubiquitin ligase machinery. This proximity supports pirin ubiquitination and depletion at low cellular concentrations, making the compound useful for chemical biology studies of pirin function. In targeted protein degradation workflows, CCT367766 formic can help evaluate pirin-dependent phenotypes, degradation selectivity, CRBN engagement, ternary-complex productivity, and the broader utility of PROTAC approaches for underexplored proteins.
Applications• PROTAC-Driven Oncogenic Protein Degradation: CCT367766 formic is a potent PROTAC compound designed to facilitate the targeted degradation of oncogenic proteins, making it an invaluable tool for cancer research. By promoting the ubiquitination and subsequent proteasomal degradation of specific cancer-related proteins, this compound aids in elucidating the roles of these proteins in tumorigenesis.
• Targeted Degradation in Neurodegenerative Research: Leveraging CCT367766 formic in neurodegenerative disease models enables researchers to selectively degrade proteins implicated in disease progression. This application facilitates the study of protein homeostasis and its impact on neuronal health, offering insights into potential therapeutic targets for conditions such as Alzheimer's and Parkinson's disease.
• Mechanistic Studies of E3 Ligase Function: CCT367766 formic serves as an effective probe for investigating the mechanistic aspects of E3 ubiquitin ligase activity. By selectively recruiting specific ligases to target proteins, researchers can dissect the pathways and interactions involved in ubiquitin-mediated protein degradation, enhancing our understanding of cellular protein quality control systems.
• PROTAC-Mediated Signal Transduction Modulation: Utilize CCT367766 formic to study the effects of targeted protein degradation on cellular signaling pathways. This application allows for the precise modulation of signaling proteins, aiding in the dissection of complex signaling networks and their roles in various physiological and pathological processes.
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
Please contact us with any specific requirements and we will get back to you as soon as possible.