PROTAC ER Degrader-3 is a sophisticated chemical tool designed for the targeted degradation of estrogen receptors (ER), pivotal in the study of hormone-driven cancers. This molecule features a dual-binding structure: one moiety specifically binds to the estrogen receptor, while the other is conjugated to an E3 ubiquitin ligase ligand, facilitating the recruitment of the ubiquitin-proteasome system. The strategic design of PROTAC ER Degrader-3 enables it to effectively bridge the target protein and the E3 ligase, promoting ubiquitination and subsequent proteasomal degradation of the ER. This degradation mechanism allows for the selective downregulation of ER levels, providing a powerful approach to investigate estrogen receptor biology and its implications in cancer progression. As a valuable asset in PROTAC-based research, PROTAC ER Degrader-3 is instrumental in exploring the dynamics of protein degradation pathways and offers insights into the development of novel therapeutic strategies for ER-related pathologies. Researchers can leverage this tool to dissect the intricacies of targeted protein degradation and its potential applications in drug discovery.
Structure of 2158322-29-1
* 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: Targets estrogen receptor alpha (ERα) for experimental targeted protein degradation studies.
Binding Site: Binds the ERα ligand-binding domain and cereblon thalidomide-binding pocket to support productive ternary complex formation.
Mechanism of Action: PROTAC ER Degrader-3 is designed for use in PROTAC or targeted protein degradation experiments directed toward estrogen receptor alpha (ERα). The bifunctional molecule links a target-recognition element to cereblon, 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 Estrogen Receptor Degradation: PROTAC ER Degrader-3 is designed to selectively target and degrade estrogen receptors, offering a powerful tool for researchers studying hormone-driven cancers. This approach allows for the investigation of estrogen receptor functions and the development of new therapeutic strategies by eliminating these receptors at the protein level.
• Targeted Protein Degradation in Cancer Research: Utilize PROTAC ER Degrader-3 to explore the mechanisms of targeted protein degradation in cancer cells. By degrading specific proteins, researchers can dissect signaling pathways and identify potential therapeutic targets, advancing the understanding of cancer biology and treatment.
• Investigating Hormone Receptor Signaling: The use of PROTAC ER Degrader-3 enables detailed studies on the role of estrogen receptors in cellular signaling. This tool facilitates the examination of downstream effects and interactions, providing insights into hormone receptor dynamics and their implications in various physiological and pathological processes.
• Development of Novel Therapeutic Approaches: With PROTAC ER Degrader-3, researchers can innovate therapeutic approaches by targeting proteins previously considered undruggable. This strategy expands the potential for drug discovery and the development of treatments that specifically degrade disease-associated proteins.
* 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.