674799-96-3

Basic information

• Product Name: O6-[4-(AMINOMETHYL)BENZYL]GUANINE
• Synonyms: 1H-Purin-2-amine,-[[4-(aminomethyl)phenyl]methoxy] 6-((4-(Aminomethyl)benzyl)o xy)-7H-purin-2-amine;6-(4-(aminomethyl)benzyloxy)-9H-purin-2-amine;6-((4-(Aminomethyl);6-[[4-(AMinoMethyl)phenyl]Methoxy]-1H-purin-2-aMine;6-((4-(AMinoMethyl)benzyl)oxy)-7H-purin-2-aMine;6-[[4-(Aminomethyl)phenyl]methoxy]-7H-purin-2-amine;O-[4-(Aminomethyl)benzyl]guanine;H-Purin-2-amine,-[[4-(aminomethyl)phenyl]methoxy]
• CAS NO: 674799-96-3
• Molecular Formula: C₁₃H₁₄N₆O
• Molecular Weight: 270.29
• Product Categories: Nitric Oxide Reagents;Cross Linking Reagents;Amines;Aromatics;Heterocycles
• Mol File: 674799-96-3.mol

Chemical Properties

• Melting Point: >240°C(dec.)
• Boiling Point: 669.9±65.0 °C(Predicted)
• Appearance: /
• Density: 1.433±0.06 g/cm3 (20 ºC 760 Torr)
• Refractive Index: 1.748
• Storage Temp.: -20°C Freezer
• Solubility: DMSO (Slightly, Heated, Sonicated), Methanol (Slightly, Heated)
• PKA: 9.54±0.10(Predicted)
• Stability: Hygroscopic
• CAS DataBase Reference: O6-[4-(AMINOMETHYL)BENZYL]GUANINE(CAS DataBase Reference)
• NIST Chemistry Reference: O6-[4-(AMINOMETHYL)BENZYL]GUANINE(674799-96-3)
• EPA Substance Registry System: O6-[4-(AMINOMETHYL)BENZYL]GUANINE(674799-96-3)

Safety Data

• Hazardous Substances Data: 674799-96-3(Hazardous Substances Data)

Usage

Chemical Properties

White Solid

Uses

A cross linker

InChI:InChI=1/C13H14N6O/c14-5-8-1-3-9(4-2-8)6-20-12-10-11(17-7-16-10)18-13(15)19-12/h1-4,7H,5-6,14H2,(H3,15,16,17,18,19)

Upstream product

• 130029-61-7 4-[[(2,2,2-trifluoroacetyl)amino]methyl]benzoic acid 
• 56-91-7 p-aminomethylbenzoic acid 
• 10310-21-1 2-amino-6-chloropurine 
• 171723-95-8 2,2,2-trifluoro-N-[[4-(hydroxymethyl)phenyl]methyl]acetamide 
• 39895-56-2 4-hydroxymethyl-benzylamine 
• 680622-70-2 N-[ [4-[(2-amino-7H-purin-6-yl)oxymethyl]phenyl]methyl]-2,2,2-trifluoroacetamide 

Downstream Products

• 1384575-50-1 C₄₆H₄₃BF₂N₁₀O₁₁ 
• 1384575-53-4 C₄₆H₄₅BF₂N₈O₇ 

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.

Highly activatable and environment-insensitive optical highlighters for selective spatiotemporal imaging of target proteins

Optical highlighters are photoactivatable fluorescent molecules that exhibit pronounced changes in their spectral properties in response to irradiation with light of a specific wavelength and intensity. Here, we present a novel design strategy for a new class of caged BODIPY (4,4-difluoro-4-bora-3a, 4a-diaza-s-indacene) fluorophores, based on the use of photoremovable protecting groups (PRPGs) with high reduction potentials that serve as both a photosensitive unit and a fluorescence quencher via photoinduced electron transfer (PeT). 2,6-Dinitrobenzyl (DNB)-caged BODIPY was efficiently photoactivated, with activation ratios exceeding 600-fold in aqueous solutions. We then combined this photoactivatable fluorophore with a SNAP (mutant of O 6-alkylguanine DNA alkyltransferase) ligand to obtain a small-molecule-based optical highlighter for visualization of protein dynamics, using the well-established SNAP tag technology. As proof of concept, we demonstrate spatiotemporal imaging of the fusion protein of epidermal growth factor receptor (EGFR) with SNAP tag in living cells. We also demonstrate highlighting of cells of interest in live zebrafish embryos, using the fusion protein of histone 2A with SNAP tag.