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N-(p-tolyl)ethenesulfonamide is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

59902-87-3

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59902-87-3 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 59902-87-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 5,9,9,0 and 2 respectively; the second part has 2 digits, 8 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 59902-87:
(7*5)+(6*9)+(5*9)+(4*0)+(3*2)+(2*8)+(1*7)=163
163 % 10 = 3
So 59902-87-3 is a valid CAS Registry Number.

59902-87-3Downstream Products

59902-87-3Relevant academic research and scientific papers

Visible-Light-Promoted Radical Cyclization of N -Arylvinylsulfonamides: Synthesis of CF 3/CHF 2/CH 2CF 3-Containing 1,3-Dihydrobenzo[ c ]isothiazole 2,2-Dioxide Derivatives

Vytla, Devaiah,Kaliyaperumal, Kumargurubaran,Velayuthaperumal, Rajeswari,Shaw, Parinita,Gautam, Raj,Mathur, Arvind,Roy, Amrita

supporting information, p. 667 - 682 (2021/11/13)

A photocatalyzed and highly efficient trifluoromethylation of N-arylvinylsulfonamides using commercially available CF3SO2Cl as the trifluoromethyl radical source under blue LEDs is reported. The reaction proceeds through radical cyclization under mild con

Selective lysine modification of native peptides: Via aza-Michael addition

Chen, Hongli,Huang, Rong,Li, Zhihong,Zhu, Wei,Chen, Jiakang,Zhan, Yuexiong,Jiang, Biao

supporting information, p. 7339 - 7345 (2017/09/25)

A series of vinylsulfonamides were synthesized and screened for site-selective modification of the ?-amino group of lysine-bearing free α-amine residues. N-Methyl-N-phenylethenesulfonamide has emerged as an applicable reagent and has been developed for efficient and highly selective modification of the lysine residue of native peptides in the presence of a free N-terminus via aza-Michael addition. We demonstrated that functional N-phenylvinylsulfonamide derivatives with a fluorescent moiety or drug could also be conjugated to the lysine residue of octreotide and insulin with high specificity, without modifying the N-terminus. Our method provides a promising strategy for site-selective lysine functionalization in native peptides with a free N-terminus.

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