31123-05-4 Usage
General Description
3,4-BIS-BENZYLOXY-BENZALDEHYDE OXIME is a chemical compound that is commonly used as an organic intermediate in the synthesis of various pharmaceuticals, agrochemicals, and organic compounds. It is a yellow to light brown solid that is stable under normal conditions. 3,4-BIS-BENZYLOXY-BENZALDEHYDE OXIME is known for its use as a chelating agent in various chemical processes, as well as for its ability to form coordination complexes with metal ions. It is also used as a reagent in organic reactions, particularly in the preparation of nitrogen-containing compounds. Additionally, 3,4-BIS-BENZYLOXY-BENZALDEHYDE OXIME has been studied for its potential applications in the development of new materials and for its antimicrobial and antioxidant properties.
Check Digit Verification of cas no
The CAS Registry Mumber 31123-05-4 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,1,1,2 and 3 respectively; the second part has 2 digits, 0 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 31123-05:
(7*3)+(6*1)+(5*1)+(4*2)+(3*3)+(2*0)+(1*5)=54
54 % 10 = 4
So 31123-05-4 is a valid CAS Registry Number.
InChI:InChI=1/C21H19NO3/c23-22-14-19-11-12-20(24-15-17-7-3-1-4-8-17)21(13-19)25-16-18-9-5-2-6-10-18/h1-14,23H,15-16H2/b22-14+
31123-05-4Relevant articles and documents
Design and synthesis of neolamellarin a derivatives targeting heat shock protein 90
Jiang, Long,Yin, Ruijuan,Wang, Xueting,Dai, Jiajia,Li, Jing,Jiang, Tao,Yu, Rilei
, p. 24 - 33 (2017/04/21)
In this study, we designed and synthesized a novel family of neolamellarin A derivatives that showed high inhibitory activity toward heat shock protein 90 (Hsp90), a kinase associated with cell proliferation. The 3,4-bis(catechol)pyrrole scaffold and the benzyl group with methoxy modification at N position of pyrrole are essential to the Hsp90 inhibitory activity and cytotoxicity of these compounds. Western blot analysis demonstrated that these compounds induced dramatic depletion of the examined client proteins of Hsp90, and accelerated cancer cell apoptosis. Docking simulations suggested that the binding mode of 9p was similar to that of the VER49009, a potent inhibitor of Hsp90. Further molecular dynamics simulation indicated that the hydrophobic interactions as well as the hydrogen bonds contributed to the high affinity of 9p to Hsp90.
