19996-02-2 Usage
Chemical family
Anthracene derivatives
Structural feature
Chlorinated derivative of anthracene with a hydroxyl group attached to the ninth carbon
Common use
Synthesis of organic compounds and pharmaceuticals
Reactivity
Unique structure and reactivity
Precursor
Production of dyes, pigments, and optical brighteners
Potential applications
Organic electronics and materials science
Electronic properties
Has electronic properties that make it useful in the field of organic electronics
Optical properties
Has optical properties that make it useful in the field of materials science
Industry applications
Wide range of potential uses and applications in various industries
Check Digit Verification of cas no
The CAS Registry Mumber 19996-02-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,9,9,9 and 6 respectively; the second part has 2 digits, 0 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 19996-02:
(7*1)+(6*9)+(5*9)+(4*9)+(3*6)+(2*0)+(1*2)=162
162 % 10 = 2
So 19996-02-2 is a valid CAS Registry Number.
InChI:InChI=1/C15H11ClO/c16-15-12-7-3-1-5-10(12)14(9-17)11-6-2-4-8-13(11)15/h1-8,17H,9H2
19996-02-2Relevant articles and documents
Determination of protonation states of iminosugar-enzyme complexes using photoinduced electron transfer
Wang, Bo,Olsen, Jacob Ingemar,Laursen, Bo W.,Navarro Poulsen, Jens Christian,Bols, Mikael
, p. 7383 - 7393 (2017)
A series of N-alkylated analogues of 1-deoxynojirimycin containing a fluorescent 10-chloro-9-anthracene group in the N-alkyl substituent were prepared. The anthracene group acted as a reporting group for protonation at the nitrogen in the iminosugar because an unprotonated amine was found to quench fluorescence by photoinduced electron transfer. The new compounds were found to inhibit β-glucosidase from Phanerochaete chrysosporium and α-glucosidase from Aspergillus Niger, with Ki values in the low micro- to nanomolar range. Fluorescence and inhibition versus pH studies of the β-glucosidase-iminosugar complexes revealed that the amino group in the inhibitor is unprotonated when bound, while one of the active site carboxylates is protonated.
