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676348-45-1

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676348-45-1 Usage

General Description

(2-CHLORO-4-FLUORO-PHENYL)-ACETYL CHLORIDE is a chemical compound with the molecular formula C8H6ClFO and a molar mass of 166.58 g/mol. It is a chlorinated acetyl chloride derivative with a halogenated benzene ring. (2-CHLORO-4-FLUORO-PHENYL)-ACETYL CHLORIDE is commonly used in organic synthesis as a reagent for introducing the (2-chloro-4-fluorophenyl)acetyl group into various organic molecules. It is a versatile building block for the preparation of pharmaceuticals, agrochemicals, and other fine chemicals. Additionally, it is used in the production of dyes, perfumes, and other organic compounds. Due to its acetyl chloride functional group, it is a reactive compound that requires careful handling and storage.

Check Digit Verification of cas no

The CAS Registry Mumber 676348-45-1 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 6,7,6,3,4 and 8 respectively; the second part has 2 digits, 4 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 676348-45:
(8*6)+(7*7)+(6*6)+(5*3)+(4*4)+(3*8)+(2*4)+(1*5)=201
201 % 10 = 1
So 676348-45-1 is a valid CAS Registry Number.

676348-45-1SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 18, 2017

Revision Date: Aug 18, 2017

1.Identification

1.1 GHS Product identifier

Product name 2-(2-chloro-4-fluorophenyl)acetyl chloride

1.2 Other means of identification

Product number -
Other names (2-Chloro-4-fluorophenyl)acetyl chloride

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:676348-45-1 SDS

676348-45-1Downstream Products

676348-45-1Relevant articles and documents

Identification of BR102910 as a selective fibroblast activation protein (FAP) inhibitor

Jung, Hui Jin,Nam, Eun Hye,Park, Jin Young,Ghosh, Prithwish,Kim, In Su

supporting information, (2021/02/26)

Fibroblast activation protein (FAP) belongs to the family of prolyl-specific serine proteases and displays both exopeptidase and endopeptidase activities. FAP expression is undetectable in most normal adult tissues, but is greatly upregulated in sites of tissue remodeling, which include fibrosis, inflammation and cancer. Due to its restricted expression pattern and dual enzymatic activities, FAP inhibition is investigated as a therapeutic option for several diseases. In the present study, we described the structure–activity relationship of several synthesized compounds against DPPIV and prolyl oligopeptidase (PREP). In particular, BR102910 (compound 24) showed nanomolar potency and high selectivity. Moreover, the in vivo FAP inhibition study of BR102910 (compound 24) using C57BL/6J mice demonstrated exceptional profiles and satisfactory FAP inhibition efficacy. Based on excellent in vitro and in vivo profiles, the potential of BR102910 (compound 24) as a lead candidate for the treatment of type 2 diabetes is considered.

Phosphonic acid analogs of fluorophenylalanines as inhibitors of human and porcine aminopeptidases N: Validation of the importance of the substitution of the aromatic ring

Dziuk, B?a?ej,Kafarski, Pawe?,Pirat, Jean-Luc,Talma, Micha?,Wanat, Weronika

, (2020/05/04)

A library of phosphonic acid analogs of phenylalanine substituted with fluorine, chlorine and trifluoromethyl moieties on the aromatic ring was synthesized and evaluated for inhibitory activity against human (hAPN) and porcine (pAPN) aminopeptidases. Fluorogenic screening indicated that these analogs are micromolar or submicromolar inhibitors, both enzymes being more active against hAPN. In order to better understand the mode of the action of the most active compounds, molecular modeling was used. It confirmed that aminophosphonic portion of the enzyme is bound nearly identically in the case of all the studied compounds, whereas the difference in activity results from the placement of aromatic side chain of an inhibitor. Interestingly, both enantiomers of the individual compounds are usually bound quite similarly.

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