PROTAC HSP90 degrader BP3

 CAS No.: 2669072-88-0  Cat No.: BP-400183 4.5  

PROTAC HSP90 degrader BP3 is a novel chemical compound designed for the targeted degradation of the Heat Shock Protein 90 (HSP90), a molecular chaperone pivotal in the stability and function of numerous client proteins involved in cancer progression. This degrader features a bifunctional design, with one moiety binding selectively to the ATP-binding site of HSP90, while the other moiety is linked to an E3 ubiquitin ligase ligand. This strategic configuration facilitates the recruitment of the E3 ligase to the HSP90 complex, promoting ubiquitination and subsequent proteasomal degradation of HSP90. By harnessing the PROTAC technology, BP3 effectively disrupts HSP90's chaperoning activity, leading to the destabilization of oncogenic client proteins. In research applications, PROTAC HSP90 degrader BP3 serves as a powerful tool for elucidating the role of HSP90 in cellular processes and offers a promising avenue for investigating therapeutic strategies targeting protein homeostasis in cancer. Its ability to modulate protein levels precisely makes it invaluable in the study of targeted protein degradation mechanisms.

PROTAC HSP90 degrader BP3

Structure of 2669072-88-0

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PROTAC
Molecular Formula
C32H29ClN8O5
Molecular Weight
641.08
Appearance
Solid

* For research and manufacturing use only. Not for human or clinical use.

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Appearance
Solid
Storage
Store at -20°C
Mechanism

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 HSP90 degrader BP3 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 HSP90 Degradation: PROTAC HSP90 degrader BP3 is designed to facilitate the targeted degradation of HSP90, a critical chaperone protein involved in protein folding and stability. This application enables researchers to explore the functional consequences of HSP90 depletion, providing insights into its role in cellular homeostasis and disease mechanisms.

• Cancer Research via Targeted Degradation: By employing PROTAC HSP90 degrader BP3, scientists can investigate the therapeutic potential of degrading HSP90 in cancer cells. This approach aids in understanding how disrupting HSP90's chaperone activity affects tumor growth and survival, thereby contributing to the development of novel cancer treatment strategies.

• Studying Proteostasis Networks: The use of PROTAC HSP90 degrader BP3 allows for the examination of proteostasis networks by targeting HSP90 for degradation. Researchers can analyze the downstream effects on client proteins and co-chaperones, offering valuable insights into the complex interactions within cellular protein quality control systems.

• Mechanistic Insights into Protein Degradation: PROTAC HSP90 degrader BP3 serves as a tool for elucidating the mechanisms of targeted protein degradation. By observing the selective degradation of HSP90, researchers can gain a deeper understanding of the ubiquitin-proteasome system and its application in regulating protein levels in various biological contexts.

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Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2

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Tip: Chemical formula is case sensitive. C22H30N4O c22h30n40
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