1335107-30-6

Basic information

• Product Name: (2,2,5-trimethyl-1,3-dioxan-5-yl)methyl (3-nitrophenyl)methanesulfonate
• CAS NO: 1335107-30-6
• Molecular Weight: 359.4
• Mol File: 1335107-30-6.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: (2,2,5-trimethyl-1,3-dioxan-5-yl)methyl (3-nitrophenyl)methanesulfonate(CAS DataBase Reference)
• NIST Chemistry Reference: (2,2,5-trimethyl-1,3-dioxan-5-yl)methyl (3-nitrophenyl)methanesulfonate(1335107-30-6)
• EPA Substance Registry System: (2,2,5-trimethyl-1,3-dioxan-5-yl)methyl (3-nitrophenyl)methanesulfonate(1335107-30-6)

Safety Data

• Hazardous Substances Data: 1335107-30-6(Hazardous Substances Data)

Upstream product

• 619-23-8 3-Nitrobenzyl chloride 
• 77472-39-0 (3-nitrophenyl)methanethiol 
• 1335107-28-2 ethoxy(((3-nitrophenyl)methyl)sulfanyl)methanethione 
• 3663-46-5 5-hydroxymethyl-2,2,5-trimethyl-1,3-dioxane 
• 58032-84-1 (3-nitrophenyl)methanesulfonyl chloride 

Downstream Products

• 1335107-31-7 (2,2,5-trimethyl-1,3-dioxan-5-yl)methyl (3-aminophenyl)methanesulfonate 
• 1335107-32-8 (2,2,5-trimethyl-1,3-dioxan-5-yl)methyl (3-hydrazinylphenyl)methanesulfonate 
• 1335107-33-9 C₅₁H₆₈N₄O₉S₄ 

Relevant articles and documents

Designed to dissolve: Suppression of colloidal aggregation of Cu(I)-selective fluorescent probes in aqueous buffer and in-gel detection of a metallochaperone

Due to the lipophilicity of the metal-ion receptor, previously reported Cu(I)-selective fluorescent probes form colloidal aggregates, as revealed by dynamic light scattering. To address this problem, we have developed a hydrophilic triarylpyrazoline-based fluorescent probe, CTAP-2, that dissolves directly in water and shows a rapid, reversible, and highly selective 65-fold fluorescence turn-on response to Cu(I) in aqueous solution. CTAP-2 proved to be sufficiently sensitive for direct in-gel detection of Cu(I) bound to the metallochaperone Atox1, demonstrating the potential for cation-selective fluorescent probes to serve as tools in metalloproteomics for identifying proteins with readily accessible metal-binding sites.