891-35-0

Basic information

• Product Name: 4-AMINO-N-(4-METHOXY-PHENYL)-BENZAMIDE
• Synonyms: 4-Amino-N-(4-methoxyphenyl)
• CAS NO: 891-35-0
• Molecular Formula: C₁₄H₁₄N₂O₂
• Molecular Weight: 242.28
• Mol File: 891-35-0.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 360.2°C at 760 mmHg
• Flash Point: 171.6°C
• Appearance: /
• Density: 1.245g/cm³
• Vapor Pressure: 2.26E-05mmHg at 25°C
• Refractive Index: 1.658
• Storage Temp.: 2-8°C
• CAS DataBase Reference: 4-AMINO-N-(4-METHOXY-PHENYL)-BENZAMIDE(CAS DataBase Reference)
• NIST Chemistry Reference: 4-AMINO-N-(4-METHOXY-PHENYL)-BENZAMIDE(891-35-0)
• EPA Substance Registry System: 4-AMINO-N-(4-METHOXY-PHENYL)-BENZAMIDE(891-35-0)

Safety Data

• Hazardous Substances Data: 891-35-0(Hazardous Substances Data)

Usage

General Description

4-AMINO-N-(4-METHOXY-PHENYL)-BENZAMIDE is a chemical compound that belongs to the class of benzamides. It is characterized by a benzamide core structure with an amino group and a methoxy group attached to the phenyl ring. 4-AMINO-N-(4-METHOXY-PHENYL)-BENZAMIDE has potential applications in medicinal chemistry and pharmaceutical research due to its ability to interact with biological systems and modulate various biochemical processes. Its unique structure and properties make it a valuable building block for the synthesis of other organic compounds with potential therapeutic applications. Additionally, it may have potential uses in fields such as drug discovery, chemical biology, and material sciences due to its diverse reactivity and potential for creating novel chemical entities.

InChI:InChI=1/C14H14N2O2/c1-18-13-8-6-12(7-9-13)16-14(17)10-2-4-11(15)5-3-10/h2-9H,15H2,1H3,(H,16,17)

Upstream product

• 104-94-9 4-methoxy-aniline 
• 122-04-3 4-nitro-benzoyl chloride 
• 150-13-0 4-amino-benzoic acid 
• 16106-38-0 4-aminobenzoyl chloride 
• 62-23-7 4-nitro-benzoic acid 

Downstream Products

• 1447816-85-4 4-[(1,1-dioxidobenzo[d]isothiazol-3-yl)amino]-N-(4-methoxyphenyl)benzamide 

Relevant articles and documents

Design, synthesis and biological evaluation of novel 2-phenyl pyrimidine derivatives as potent Bruton's tyrosine kinase (BTK) inhibitors

BTK is an effective target for the treatment of B-cell malignant tumors and autoimmune diseases. In this work, a series of 2-phenyl pyrimidine derivatives were prepared and their preliminary in vitro activities on B-cell leukemia cells as well as the BTK enzyme were determined. The results showed that compound 11g displayed the best inhibitory activity on BTK with an inhibition rate of 82.76% at 100 nM and excellent anti-proliferation activity on three B-cell leukemia lines (IC50 = 3.66 μM, 6.98 μM, and 5.39 μM against HL60, Raji and Ramos, respectively). Besides, the flow cytometry analysis results indicated that 11g inhibited the proliferation of the Raji cells in a dose- and time-dependent manner, and blocked the Ramos cells at the G0/G1 phase, which is in accordance with the positive control ibrutinib. The mechanism investigation demonstrated that 11g could inhibit the phosphorylation of BTK and its downstream substrate phospholipase γ2 (PLCγ2). All these results showed that 11g was a promising lead compound that merited further optimization as a novel class of BTK inhibitor for the treatment of B-cell lymphoblastic leukemia.

2-phenylpyrimidine compounds, preparation method and medical application

The invention belongs to the field of medicines and particularly relates to 2-phenylpyrimidine compounds and pharmacologically-acceptable salts thereof and an isotope marker. The invention also discloses a pharmaceutical composition containing the substances and application of the pharmaceutical composition for treating diseases related with protein kinase activity, such as cancer and inflammation. (The formula is shown in the description).

Identification of Multiple Structurally Distinct, Nonpeptidic Small Molecule Inhibitors of Protein Arginine Deiminase 3 Using a Substrate-Based Fragment Method

The protein arginine deiminases (PADs) are a family of enzymes that catalyze the post-translational hydrolytic deimination of arginine residues. Four different enzymologically active PAD subtypes have been characterized and exhibit tissue-specific expression and association with a number of different diseases. In this Article we describe the development of an approach for the reliable discovery of low molecular weight, nonpeptidic fragment substrates of the PADs that then can be optimized and converted to mechanism-based irreversible PAD inhibitors. The approach is demonstrated by the development of potent and selective inhibitors of PAD3, a PAD subtype implicated in the neurodegenerative response to spinal cord injury. Multiple structurally distinct inhibitors were identified with the most potent inhibitors having >10,000 min-1 M-1 kinact/KI values and ≥10-fold selectivity for PAD3 over PADs 1, 2, and 4. (Figure Presented).