220510-16-7

Basic information

• Product Name: NSCI
• Synonyms: NSCI
• CAS NO: 220510-16-7
• Molecular Formula: C₂₆H₂₄N₂O₅S
• Molecular Weight: 507.565
• Mol File: 220510-16-7.mol

Chemical Properties

• Appearance: /
• Storage Temp.: −20°C
• CAS DataBase Reference: NSCI(CAS DataBase Reference)
• NIST Chemistry Reference: NSCI(220510-16-7)
• EPA Substance Registry System: NSCI(220510-16-7)

Safety Data

• Hazardous Substances Data: 220510-16-7(Hazardous Substances Data)

Upstream product

• 174213-51-5 (S)-tert-butyl 2-(phenoxymethyl)pyrrolidine-1-carboxylate 
• 69610-40-8 N-(tert-butoxycarbonyl)-L-prolinol 
• 80789-74-8 5-isatinsulfonic acid sodium salt 
• 86661-32-7 (S)-tert-butyl 2-((tosyloxy)methyl)pyrrolidine-1-carboxylate 
• 100-39-0 benzyl bromide 
• 220509-98-8 5-(2-phenoxymethyl-pyrrolidine-1-sulfonyl)-1H-indole-2,3-dione 
• 132898-96-5 5-chlorosulfonylisatin 

Relevant articles and documents

ISATIN ANALOGUES AND USES THEREFOR

Novel isatin analogues, including isatin analogues comprising Michael Acceptors (IMAs) are disclosed. Further disclosed are methods of synthesis of the isatin analogues, and uses of the analogues, including inhibition of caspase-3 and caspase-7, and in vi

Isatin sulfonamide analogs containing a Michael addition acceptor: A new class of caspase 3/7 inhibitors

A series of isatin sulfonamide analogs having a Michael acceptor were prepared and their potencies for inhibiting caspase-1, -3, -6, -7, and -8 were evaluated. These compounds have nanomolar potency for inhibiting the executioner caspases, caspase-3 and c

N-benzylisatin sulfonamide analogues as potent caspase-3 inhibitors: Synthesis, in vitro activity, and molecular modeling studies

A number of isatin sulfonamide analogues were prepared and their potencies for inhibiting caspase-1, -3, -6, -7, and -8 were evaluated in vitro. Several compounds displaying a nanomolar potency for inhibiting the executioner caspases, caspase-3 and caspas

Potent and selective nonpeptide inhibitors of caspases 3 and 7

5-Dialkylaminosulfonylisatins have been identified as potent, nonpeptide inhibitors of caspases 3 and 7. The most active compound within this series (34) inhibited caspases 3 and 7 in the 2-6 nM range and exhibited approximately 1000-fold selectivity for caspases 3 and 7 versus a panel of five other caspases (1, 2, 4, 6, and 8) and was at least 20-fold more selective versus caspase 9. Sequence alignments of the active site residues of the caspases strongly suggest that the basis of this selectivity is due to binding in the S2 subsite comprised of residues Tyr204, Trp206, and Phe256 which are unique to caspases 3 and 7. These compounds inhibit apoptosis in three cell-based models: human Jurkat T cells, human chondrocytes, and mouse bone marrow neutrophils.