HaloPROTAC-E is a HaloTag-directed degrader designed to induce degradation of Halo-tagged proteins, including endoplasmic-reticulum-localized HaloTag fusion proteins. Its HaloTag-reactive or HaloTag-binding module engages the engineered HaloTag site on the fusion protein, while the degrader architecture recruits cellular degradation machinery through an E3-ligase-recruiting component. Public sources emphasize reversible degradation of Halo-tagged SGK3 and VPS34, indicating utility for proteins localized in challenging intracellular compartments. In PROTAC design, HaloPROTAC-E is a tag-based degradation tool, similar in concept to dTAG systems, and does not require an endogenous ligand for the protein of interest. Mechanistically, it brings the HaloTag fusion protein into proximity with ubiquitination machinery, supporting proteasome-dependent target depletion. It is valuable for studying compartment-specific degradation, tag-based target validation, protein turnover, degradation reversibility, and engineered systems where direct small-molecule target binders are unavailable.
Structure of 2365478-58-4
* For research and manufacturing use only. Not for human or clinical use.
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Target: Targets HaloTag fusion proteins for experimental targeted protein degradation studies.
Binding Site: Binds the HaloTag chloroalkane-binding tunnel and VHL substrate-recognition domain to support productive ternary complex formation.
Mechanism of Action: HaloPROTAC-E is designed for use in PROTAC or targeted protein degradation experiments directed toward HaloTag fusion proteins. The bifunctional molecule links a target-recognition element to VHL, promoting proximity between the protein of interest and ubiquitination machinery. Productive ternary-complex formation can drive polyubiquitination and proteasome-dependent target depletion, allowing researchers to compare pharmacological inhibition with protein removal. It is suitable for evaluating degradation potency, kinetics, pathway selectivity, and downstream signaling consequences in engineered or disease-relevant cellular models.
Applications• PROTAC-Mediated Protein Degradation: HaloPROTAC-E is designed for the targeted degradation of HaloTag-fused proteins, enabling researchers to study protein function by selectively removing proteins of interest from cells. This approach facilitates the investigation of protein roles in cellular processes and the validation of potential therapeutic targets.
• Targeted Degradation in Drug Discovery: By employing HaloPROTAC-E, scientists can explore the degradation of specific proteins implicated in disease pathways. This aids in the identification of novel drug targets and enhances the understanding of protein dynamics within complex biological systems, accelerating drug discovery efforts.
• Functional Proteomics with PROTACs: HaloPROTAC-E serves as a powerful tool in functional proteomics, allowing for the rapid and reversible degradation of proteins. This capability enables the study of protein interactions and cellular pathways, providing insights into the mechanistic underpinnings of cellular functions and disease mechanisms.
• Investigating Protein Turnover: Researchers use HaloPROTAC-E to probe the mechanisms of protein turnover and stability within cells. By selectively degrading proteins, it is possible to dissect the pathways involved in protein homeostasis and understand how dysregulation contributes to various diseases, offering potential avenues for therapeutic intervention.
* 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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