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41978-14-7

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41978-14-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 41978-14-7 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 4,1,9,7 and 8 respectively; the second part has 2 digits, 1 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 41978-14:
(7*4)+(6*1)+(5*9)+(4*7)+(3*8)+(2*1)+(1*4)=137
137 % 10 = 7
So 41978-14-7 is a valid CAS Registry Number.

41978-14-7SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 14, 2017

Revision Date: Aug 14, 2017

1.Identification

1.1 GHS Product identifier

Product name N-(1,3-Benzothiazol-2-ylsulfanyl)-2-propen-1-amine

1.2 Other means of identification

Product number -
Other names Benzothiazyl-2-allylsulfenamid

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:41978-14-7 SDS

41978-14-7Downstream Products

41978-14-7Relevant articles and documents

Novel sulfenamides as promising acetylcholinesterase inhibitors

Proenca, Carla,Serralheiro, M. Luisa,Araujo, M. Eduarda,Pamplona, Teresa,Santos, Susana,Santos, M. Soledade,Frazao, Fatima

experimental part, p. 1287 - 1294 (2012/01/12)

Several sulfenamide derivatives were designed as possible acetylcholinesterase (AChE) inhibitors. New sulfenamides were synthesized and proved to be stable under the physiological conditions used in the enzymatic assays. N-benzyl-2-benzoxazolylsulfenamide (8) and N-benzyl-2- benzimidazolylsulfenamide (9) revealed anti-AChE activity with IC50 values of 0.6 and 0.8 μM, respectively, values of the same magnitude as those reported for galantamine and tacrine. The affinity for the biological site was evaluated in terms of interaction/partition toward sodium dodecyl sulfate (SDS) micelles. The inhibitory activity profiles were reasoned in terms of both partition toward a hydrophobic anionic environment and molecular geometry. The X-CSN dihedral angle deviations from collinearity stood out as a major parameter linked to enzyme specificity. Copyright

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