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4-([(3-FLUOROPHENYL)SULFONYL]AMINO)BENZOIC ACID is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

708293-25-8

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708293-25-8 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 708293-25-8 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 7,0,8,2,9 and 3 respectively; the second part has 2 digits, 2 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 708293-25:
(8*7)+(7*0)+(6*8)+(5*2)+(4*9)+(3*3)+(2*2)+(1*5)=168
168 % 10 = 8
So 708293-25-8 is a valid CAS Registry Number.

708293-25-8Downstream Products

708293-25-8Relevant academic research and scientific papers

Synthesis of aminophenylhydroxamate and aminobenzylhydroxamate derivatives and in vitro screening for antiparasitic and histone deacetylase inhibitory activity

Loeuillet,Touquet,Oury,Eddaikra,Pons,Guichou,Labesse,Sereno

, p. 59 - 66 (2018/02/10)

A series of aminophenylhydroxamates and aminobenzylhydroxamates were synthesized and screened for their antiparasitic activity against Leishmania, Trypanosoma, and Toxoplasma. Their anti-histone deacetylase (HDAC) potency was determined. Moderate to no an

Solid-phase parallel synthesis and SAR of 4-amidofuran-3-one inhibitors of cathepsin S: Effect of sulfonamides P3 substituents on potency and selectivity

Ayesa, Susana,Lindquist, Charlotta,Agback, Tatiana,Benkestock, Kurt,Classon, Bjoern,Henderson, Ian,Hewitt, Ellen,Jansson, Katarina,Kallin, Anders,Sheppard, Dave,Samuelsson, Bertil

experimental part, p. 1307 - 1324 (2009/08/08)

Highly potent and selective 4-amidofuran-3-one inhibitors of cathepsin S are described. The synthesis and structure-activity relationship of a series of inhibitors with a sulfonamide moiety in the P3 position is presented. Several members of the series show sub-nanomolar inhibition of the target enzyme as well as an excellent selectivity profile and good cellular potency. Molecular modeling of the most interesting inhibitors describes interactions in the extended S3 pocket and explains the observed selectivity towards cathepsin K.

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