24248-49-5

Basic information

• Product Name: Oxaprozin Impurity 2
• Synonyms: Oxaprozin Impurity 2;Oxaprozin Impurity
• CAS NO: 24248-49-5
• Molecular Formula: C₁₈H₁₆N₂O₂
• Molecular Weight: 292.33184
• Mol File: 24248-49-5.mol
• Article Data: 1

Chemical Properties

• Boiling Point: 500°C at 760 mmHg
• Flash Point: 256.2°C
• Appearance: /
• Density: 1.187g/cm³
• Vapor Pressure: 3.94E-10mmHg at 25°C
• Refractive Index: 1.594
• CAS DataBase Reference: Oxaprozin Impurity 2(CAS DataBase Reference)
• NIST Chemistry Reference: Oxaprozin Impurity 2(24248-49-5)
• EPA Substance Registry System: Oxaprozin Impurity 2(24248-49-5)

Safety Data

• Hazardous Substances Data: 24248-49-5(Hazardous Substances Data)

Usage

Description

Oxaprozin Impurity 2, also known as 4,5-Diphenyl-2-oxazolepropanamide, is an impurity found in Oxaprozin (O845400), which is an anti-inflammatory drug. Oxaprozin has been found to be comparable to Aspirin (A687780) in its effectiveness.

Uses

Used in Pharmaceutical Industry:
Oxaprozin Impurity 2 is used as an impurity in the production of Oxaprozin, an anti-inflammatory drug, for the reason that it is a byproduct of the synthesis process. The presence of this impurity is important to monitor and control, as it can affect the quality, safety, and efficacy of the final drug product.
Additionally, since Oxaprozin has been found to be comparable to Aspirin in its effectiveness, Oxaprozin Impurity 2 may also be relevant in the context of anti-inflammatory drug development and research, potentially leading to the discovery of new therapeutic agents or improvements in existing ones.

InChI:InChI=1/C18H16N2O2/c19-15(21)11-12-16-20-17(13-7-3-1-4-8-13)18(22-16)14-9-5-2-6-10-14/h1-10H,11-12H2,(H2,19,21)

Upstream product

• 1484-50-0 desyl bromide 

Relevant articles and documents

Discovery of the First in Vivo Active Inhibitors of the Soluble Epoxide Hydrolase Phosphatase Domain

The emerging pharmacological target soluble epoxide hydrolase (sEH) is a bifunctional enzyme exhibiting two different catalytic activities that are located in two distinct domains. Although the physiological role of the C-terminal hydrolase domain is well-investigated, little is known about its phosphatase activity, located in the N-terminal phosphatase domain of sEH (sEH-P). Herein we report the discovery and optimization of the first inhibitor of human and rat sEH-P that is applicable in vivo. X-ray structure analysis of the sEH phosphatase domain complexed with an inhibitor provides insights in the molecular basis of small-molecule sEH-P inhibition and helps to rationalize the structure-activity relationships. 4-(4-(3,4-Dichlorophenyl)-5-phenyloxazol-2-yl)butanoic acid (22b, SWE101) has an excellent pharmacokinetic and pharmacodynamic profile in rats and enables the investigation of the physiological and pathophysiological role of sEH-P in vivo.