188891-18-1

Basic information

• Product Name: Butanoic acid, 4-(4-acetyl-2-methoxy-5-nitrophenoxy)-
• CAS NO: 188891-18-1
• Molecular Formula: C13H15NO7
• Molecular Weight: 297.265
• Mol File: 188891-18-1.mol
• Article Data: 7

Chemical Properties

• CAS DataBase Reference: Butanoic acid, 4-(4-acetyl-2-methoxy-5-nitrophenoxy)-(CAS DataBase Reference)
• NIST Chemistry Reference: Butanoic acid, 4-(4-acetyl-2-methoxy-5-nitrophenoxy)-(188891-18-1)
• EPA Substance Registry System: Butanoic acid, 4-(4-acetyl-2-methoxy-5-nitrophenoxy)-(188891-18-1)

Safety Data

• Hazardous Substances Data: 188891-18-1(Hazardous Substances Data)

Upstream product

• 1285712-73-3 ethyl 4-(4-(1-chloroethyl)-2-methoxy-5-nitrophenoxy)butanoate 
• 1073426-06-8 ethyl 4-(4-(1-hydroxyethyl)-2-methoxy-5-nitrophenoxy) butanoate 
• 1031702-80-3 ethyl 4-(4-acetyl-2-methoxy-5-nitrophenoxy)butanoate 
• 498-02-2 1-(3-methoxy-4-hydroxyphenyl)ethanone 
• 174884-21-0 ethyl 4-(4-acetyl-2-methoxyphenoxy) butanoate 
• 182297-45-6 methyl 4-(4-acetyl-2-methoxy-5-nitrophenoxy)butyrate 
• 175281-79-5 methyl 4-(4-acetyl-2-methoxyphenoxy)butanoate 

Downstream Products

• 1091595-09-3 4-(4-(1-(acryloyloxy)ethyl)-2-methoxy-5-nitrophenoxy)butanoic acid 
• 175281-76-2 4-[4-(1-hydroxyethyl)-2-methoxy-5-nitrophenoxy]butanoic acid 
• 1363555-53-6 C₁₆H₁₈ClNO₇ 
• 188891-20-5 N-benzyl-4-[4-(1-hydroxyethyl)-2-methoxy-5-nitrophenoxy]butyramide 
• 188891-19-2 N-benzyl-4-(4-acetyl-2-methoxy-5-nitrophenoxy)butyramide 

Relevant articles and documents

PHOTOPROXIMITY PROFILING OF PROTEIN-PROTEIN INTERACTIONS IN CELLS

Photoactive probes and probe systems for detecting biological interactions are described. The photoactive probes include probes that combine both photocleavable and photoreactive moieties. The photoactive probe systems can include a first probe comprising a photocatalytic group and a second probe comprising a group that can act as a substrate for the reaction catalyzed by the photocatalytic group. The probes and probe systems can also include groups that can specifically bind to a binding partner on a biological entity of interest and a detectable group or a precursor thereof. The probes and probe systems can detect spatiotemporal interactions of proteins or cells. In some embodiments, the interactions can be detected in live cells. Also described are methods of detecting the biological interactions.

Photoproximity Profiling of Protein-Protein Interactions in Cells

We report a novel photoproximity protein interaction (PhotoPPI) profiling method to map protein-protein interactions in vitro and in live cells. This approach utilizes a bioorthogonal, multifunctional chemical probe that can be targeted to a genetically encoded protein of interest (POI) through a modular SNAP-Tag/benzylguanine covalent interaction. A first generation photoproximity probe, PP1, responds to 365 nm light to simultaneously cleave a central nitroveratryl linker and a peripheral diazirine group, resulting in diffusion of a highly reactive carbene nucleophile away from the POI. We demonstrate facile probe loading, and subsequent interaction- A nd light-dependent proximal labeling of a model protein-protein interaction (PPI) in vitro. Integration of the PhotoPPI workflow with quantitative LC-MS/MS enabled unbiased interaction mapping for the redox regulated sensor protein, KEAP1, for the first time in live cells. We validated known and novel interactions between KEAP1 and the proteins PGAM5 and HK2, among others, under basal cellular conditions. By contrast, comparison of PhotoPPI profiles in cells experiencing metabolic or redox stress confirmed that KEAP1 sheds many basal interactions and becomes associated with known lysosomal trafficking and proteolytic proteins like SQSTM1, CTSD, and LGMN. Together, these data establish PhotoPPI as a method capable of tracking the dynamic subcellular and protein interaction "social network" of a redox-sensitive protein in cells with high temporal resolution.

Near infrared light triggered release of biomacromolecules from hydrogels loaded with upconversion nanoparticles

Using a photosensitive hybrid hydrogel loaded with upconversion nanoparticles (UCNPs), we show that continuous-wave near-infrared (NIR) light (980 nm) can be used to induce the gel-sol transition and release large, inactive biomacromolecules (protein and