HyNic-Silane is a specialized molecular glue designed to facilitate targeted protein degradation by covalently linking proteins to specific substrates. This product targets lysine residues on protein surfaces, utilizing a silane-based binding site that ensures strong and stable attachment. The molecular characteristics of HyNic-Silane include a reactive hydrazine nicotinamide (HyNic) group, which is adept at forming stable bonds with carbonyl groups, enhancing its utility in diverse biochemical environments. The primary mechanism of action for HyNic-Silane involves its role as a bifunctional linker, promoting the ubiquitination and subsequent proteasomal degradation of target proteins. This capability is pivotal for research applications focused on elucidating protein function, mapping protein interactions, and studying the cellular pathways involved in protein homeostasis. HyNic-Silane's contribution to targeted degradation studies is invaluable, offering researchers a robust tool for manipulating protein levels within cells, thereby advancing our understanding of disease mechanisms and potential therapeutic targets. Its application in experimental research provides a foundation for innovative approaches in molecular biology and biochemistry.
* 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
E3 Ligase: HyNic-Silane does not directly recruit classical E3 ligases such as CRBN, VHL, IAP, or MDM2. It is a silane-based chemical linker that introduces hydrazinonicotinamide groups onto surfaces or biomolecules, enabling covalent conjugation and indirect study of protein interactions related to ubiquitination pathways.
Target Protein: HyNic-Silane reacts with aldehyde-functionalized proteins or biomolecules via its hydrazine moiety, forming stable hydrazone bonds. It is primarily used to label, immobilize, or modify proteins for mechanistic or structural studies rather than targeting specific endogenous proteins for degradation.
Degradation Mechanism: HyNic-Silane does not inherently induce protein degradation. Any subsequent turnover of labeled or conjugated proteins occurs indirectly through endogenous cellular pathways, typically via the ubiquitin-proteasome system, without direct engagement of lysosomal degradation mechanisms.
Applications• Molecular Glue Synthesis: HyNic-Silane is pivotal in the synthesis of molecular glues that facilitate the targeted degradation of disease-associated proteins. By enabling the covalent attachment of small molecules to specific protein surfaces, it aids in the creation of stable, effective molecular glue compounds for research in protein homeostasis.
• Targeted Degradation Assays: Utilize HyNic-Silane in designing assays that evaluate the efficiency of molecular glues in promoting targeted protein degradation. Its role in binding and stabilizing ligands on protein surfaces is crucial for understanding degradation pathways and optimizing experimental conditions in proteomics research.
• Protein-Protein Interaction Studies: HyNic-Silane supports the investigation of protein-protein interactions modulated by molecular glues. By serving as a linker, it helps in forming complexes that can be analyzed to decipher interaction dynamics and the mechanistic action of molecular glues in cellular environments.
• Drug Discovery Research: In drug discovery, HyNic-Silane is instrumental in the development of novel molecular glues aimed at degrading undruggable targets. Its versatility in chemical synthesis allows researchers to explore innovative strategies for targeting proteins that are resistant to conventional therapeutic approaches.
* 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.