BCPyr is a BTK-directed PROTAC degrader described as a candidate Bruton's tyrosine kinase degrader assembled from a BTK ligand, an E3 ubiquitin-ligase ligand, and a pyrazine-containing linker. Public sources identify the target protein ligand and the E3-ligase ligand-linker components, while detailed structural information on the induced BTK–ligase ternary complex remains limited. In PROTAC design, BCPyr functions by connecting BTK recognition to E3 recruitment, thereby transforming target binding into degradation potential. Mechanistically, it is intended to bring BTK into proximity with ubiquitination machinery, leading to BTK ubiquitination and proteasome-mediated depletion. BCPyr is useful for studying BTK degradation, B-cell receptor pathway modulation, linker-dependent degrader design, nonstandard E3-recruiting chemotypes, and experimental comparisons between kinase inhibition and kinase protein removal in immune-signaling and hematologic research models.
Structure of 2669844-82-8
* For research and manufacturing use only. Not for human or clinical use.
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Target: BCPyr targets Bruton’s tyrosine kinase, including BTK-dependent signaling complexes.
Binding site: Its BTK ligand engages the kinase-domain ATP-binding catalytic pocket.
Mechanism of action: BCPyr is a PROTAC-class BTK degrader composed of a BTK-recognition ligand, linker, and E3 ubiquitin ligase-recruiting ligand. By bringing BTK into proximity with cellular ubiquitination machinery, BCPyr is designed to promote BTK polyubiquitination and proteasome-dependent depletion rather than simple catalytic inhibition. This degradation mechanism enables investigation of BTK protein dependence, kinase-independent scaffold functions, and downstream B-cell receptor signaling suppression. BCPyr is suitable for experimental studies comparing degradation kinetics, residual kinase activity, and cellular responses after physical removal of BTK protein.
Applications• PROTAC-Driven Kinase Degradation: BCPyr is instrumental in the targeted degradation of kinases, facilitating the study of kinase signaling pathways. By selectively degrading specific kinases, researchers can dissect their roles in cellular processes and identify potential therapeutic targets for diseases characterized by dysregulated kinase activity.
• Targeted Degradation in Cancer Research: BCPyr enables the exploration of oncogenic proteins via PROTAC-mediated degradation. This approach allows scientists to evaluate the effects of depleting specific cancer-related proteins, providing insights into tumorigenesis and aiding in the development of novel cancer therapies.
• PROTAC-Based Protein Interaction Studies: Utilizing BCPyr, researchers can investigate protein-protein interactions by selectively degrading one of the interacting partners. This method aids in understanding the dynamics and functional consequences of protein interactions within various cellular contexts, offering a powerful tool for elucidating complex biological networks.
• Degradation of Disease-Associated Proteins: BCPyr offers a strategic approach to degrade proteins implicated in diseases, allowing the assessment of their functional roles. By targeting these proteins for degradation, researchers can uncover mechanistic insights and identify new avenues for therapeutic intervention in disease models.
* 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
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