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3-Carboxy-benzolsulfonsaeure-, also known as 3-carboxybenzenesulfonic acid N-(2-methylphenyl)amide, is a complex organic chemical compound with the molecular formula C14H13NO4S. 3-Carboxy-benzolsulfonsaeure- is characterized by a benzene ring with a sulfonic acid group at the 3-position, a carboxylic acid group at the same position, and an amide linkage to a 2-methylphenyl group. It is a white crystalline solid that is soluble in water and has potential applications in the synthesis of pharmaceuticals and other organic compounds. The compound's structure and properties make it a versatile building block in organic chemistry, particularly in the development of new drugs and materials.

7326-78-5

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7326-78-5 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 7326-78-5 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 7,3,2 and 6 respectively; the second part has 2 digits, 7 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 7326-78:
(6*7)+(5*3)+(4*2)+(3*6)+(2*7)+(1*8)=105
105 % 10 = 5
So 7326-78-5 is a valid CAS Registry Number.

7326-78-5Downstream Products

7326-78-5Relevant academic research and scientific papers

Design and synthesis of newer N-benzimidazol-2yl benzamide analogues as allosteric activators of human glucokinase

Singh, Sukhbir,Arora, Sandeep,Dhalio, Ervon,Sharma, Neelam,Arora, Kunal,Grewal, Ajmer Singh

, p. 760 - 770 (2021)

Allosteric activators of human glucokinase (GK) had revealed significant hypoglycemic effects for therapy of type-2 diabetes (T2D) in animal as well as human models. Some newer N-benzimidazol-2yl substituted benzamide analogues were prepared and assessed for activation of GK accompanied by molecular docking investigations for predicting the bonding interactions of these derivatives with the residues in allosteric site of GK protein. Amongst the derivatives synthesized, compounds 2 and 7 strongly increased catalytic action of GK (GK activation fold >2.0 in comparison to control) in vitro. The results of in-vitro testing were supported by the molecular docking investigations of these analogues with GK protein’s allosteric site residues (showed appreciable H-bond interactions with Arg63 residue of GK). Derivatives investigated in present study afforded few lead compounds for the discovery of harmless and strong allosteric GK activating compounds for treating T2D.

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