2939-05-1

Basic information

• Product Name: 1H-IMidazole,2-(broMoMethyl)-,hydrobroMide(1:1)
• Synonyms: 1H-IMidazole,2-(broMoMethyl)-,hydrobroMide(1:1);2-(BroMoMethyl)-1H-iMidazole hydrobroMide;2-(BROMOMETHYL)-1H-IMIDAZOLE HBR
• CAS NO: 2939-05-1
• Molecular Formula: C4H6Br2N2
• Molecular Weight: 241.91184
• EINECS: -0
• Mol File: 2939-05-1.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• Storage Temp.: Inert atmosphere,Store in freezer, under -20°C
• CAS DataBase Reference: 1H-IMidazole,2-(broMoMethyl)-,hydrobroMide(1:1)(CAS DataBase Reference)
• NIST Chemistry Reference: 1H-IMidazole,2-(broMoMethyl)-,hydrobroMide(1:1)(2939-05-1)
• EPA Substance Registry System: 1H-IMidazole,2-(broMoMethyl)-,hydrobroMide(1:1)(2939-05-1)

Safety Data

• Hazardous Substances Data: 2939-05-1(Hazardous Substances Data)

Usage

General Description

The chemical "1H-IMidazole,2-(broMoMethyl)-,hydrobroMide(1:1)" is a compound composed of 1H-imidazole and bromomethyl, with a 1:1 ratio of hydrobromide. It is a solid substance that is commonly used in organic chemistry as a reagent and precursor for various chemical reactions. 1H-IMidazole,2-(broMoMethyl)-,hydrobroMide(1:1) has several industrial applications, including as a pharmaceutical intermediate and in the synthesis of organic compounds. It is important to handle this chemical with caution and follow safety guidelines due to its potential hazards and toxicity.

Upstream product

• 3724-26-3 2-hydroxymethyl-1H-imidazole 

Relevant articles and documents

Crystal Structure and Subsequent Ligand Design of a Nonriboside Partial Agonist Bound to the Adenosine A2AReceptor

In this study, we determined the crystal structure of an engineered human adenosine A2A receptor bound to a partial agonist and compared it to structures cocrystallized with either a full agonist or an antagonist/inverse agonist. The interaction between the partial agonist, belonging to a class of dicyanopyridines, and amino acids in the ligand binding pocket inspired us to develop a small library of derivatives and assess their affinity in radioligand binding studies and potency and intrinsic activity in a functional, label-free, intact cell assay. It appeared that some of the derivatives retained the partial agonist profile, whereas other ligands turned into inverse agonists. We rationalized this remarkable behavior with additional computational docking studies.