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934537-52-7

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934537-52-7 Usage

Uses

N3-(3-Bromobenzyl)pyridine-2,3-diamine is use research chemical.

Check Digit Verification of cas no

The CAS Registry Mumber 934537-52-7 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 9,3,4,5,3 and 7 respectively; the second part has 2 digits, 5 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 934537-52:
(8*9)+(7*3)+(6*4)+(5*5)+(4*3)+(3*7)+(2*5)+(1*2)=187
187 % 10 = 7
So 934537-52-7 is a valid CAS Registry Number.
InChI:InChI=1/C12H12BrN3/c13-10-4-1-3-9(7-10)8-16-11-5-2-6-15-12(11)14/h1-7,16H,8H2,(H2,14,15)

934537-52-7SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 15, 2017

Revision Date: Aug 15, 2017

1.Identification

1.1 GHS Product identifier

Product name N3-(3-Bromobenzyl)pyridine-2,3-diamine

1.2 Other means of identification

Product number -
Other names 3-N-[(3-bromophenyl)methyl]pyridine-2,3-diamine

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:934537-52-7 SDS

934537-52-7Downstream Products

934537-52-7Relevant articles and documents

Application of fragment screening by X-ray crystallography to the discovery of aminopyridines as inhibitors of β-secretase

Congreve, Miles,Aharony, David,Albert, Jeffrey,Callaghan, Owen,Campbell, James,Carr, Robin A. E.,Chessari, Gianni,Cowan, Suzanna,Edwards, Philip D.,Frederickson, Martyn,McMenamin, Rachel,Murray, Christopher W.,Patel, Sahil,Wallis, Nicola

, p. 1124 - 1132 (2007)

Fragment-based lead discovery has been successfully applied to the aspartyl protease enzyme β-secretase (BACE-1). Fragment hits that contained an aminopyridine motif binding to the two catalytic aspartic acid residues in the active site of the enzyme were the chemical starting points. Structure-based design approaches have led to identification of low micromolar lead compounds that retain these interactions and additionally occupy adjacent hydrophobic pockets of the active site. These leads form two subseries, for which compounds 4 (IC50 = 25 μM) and 6c (IC50 = 24 μM) are representative. In the latter series, further optimization has led to 8a (IC50 = 690 nM).

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