62507-86-2

Usage

Uses

Used in Pharmaceutical Industry:
3-(4-methylphenoxy)benzoic acid is used as a building block for the synthesis of various pharmaceuticals due to its chemical properties that facilitate the creation of new drug molecules.
Used in Agrochemical Industry:
In the agrochemical sector, 3-(4-methylphenoxy)benzoic acid is utilized as a precursor in the development of agrochemicals, contributing to the production of effective and safe products for agricultural applications.
Used in Dye Industry:
3-(4-methylphenoxy)benzoic acid is employed as a key component in the synthesis of dyes, where its chemical structure plays a role in the color and properties of the final dye products.
Used in Liquid Crystal Production:
As an intermediate in the production of liquid crystals, 3-(4-methylphenoxy)benzoic acid is instrumental in creating materials that are vital for display technologies and other applications requiring specific optical properties.
Used in Sunscreen Formulations:
3-(4-methylphenoxy)benzoic acid is used as a key ingredient in sunscreen formulations, where it contributes to the product's ability to protect the skin from harmful ultraviolet radiation.

Upstream product

• 106-44-5 p-cresol 
• 535-80-8 3-chlorobenzoate 
• 79124-75-7 3-(4-methylphenoxy)-benzaldehyde 

Downstream Products

• 223477-44-9 3-p-tolyloxy-benzoic acid (2-oxo-1,2-dihydro-indol-3-ylidene)-hydrazide 
• 223477-41-6 3-p-tolyloxy-benzoic acid hydrazide 
• 78303-09-0 3-p-tolyloxy-benzoic acid methyl ester 

Relevant academic research and scientific papers

Synthesis of some novel 1-aminomethyl-3-benzoylhydrazono-2-indolinones as potential antiinflammatory agents

Acid-catalysed condensation of hydrazides 3, obtained from substituted phenoxybenzoic acids 1 with indolin-2,3-dione 4, results into hydrazono-2-indolinones 5. Compounds 5 when subjected to Mannich reaction with different cyclic secondary amines yield 1-aminomethyl-3-benzoylhydrazono-2-indolinones 6 (Mannich bases). All these compounds (6a-i) exhibit significant antiinflammatory activity.

Rat hepatic microsomal aldehyde dehydrogenase. Identification of 3- and 4-substituted aromatic aldehydes as substrates of the enzyme

The rat hepatic microsomal aldehyde dehydrogenase (mALDH) metabolizes aliphatic and aromatic aldehydes to the corresponding acids with NAD as the optimal cofactor. However, dehydrogenation of the aliphatic compounds is substantially more efficient. In the present study, a series of aromatic aldehydes was evaluated as substrates of the purified mALDH so that the physicochemical factors that contribute to substrate affinity could be evaluated. Substitution of the aromatic system in the 3- and 4-positions produced relatively good substrates, but 2-substituted congeners did not undergo dehydrogenation. However, aldehydes with hydrophilic substituents in the 3- or 4-positions and those with extremely bulky substituents at both positions (e.g., 3,4-dibenzyloxy) were also poor substrates for the enzyme and dehydrogenation was undetectable. A quantitative structure-activity relationship was determined that related the logarithm of the Michaelis constants for 27 substituted aromatic aldehydes with the zero-order connectivity function of the molecule (0χ), the shapes of the 3-and 4-substituents (κ), and the electronic nature of the 4-substituent (σ). In this equation, 81% of the data variance was explained. From a consideration of the dimensions of 3-phenoxybenzaldehyde, which was a relatively good substrate, the mALDH possesses a narrow cleft within the active site that is at least 7.5 A wide and extends at least 12 A from the the catalytic residue (probably cysteine). Previously established relationships between connectivity functions and molecular polarizability suggest that dipolar interactions within the active site, as well as dispersion forces, may play a role in substrate specificity. Although optimal shapes for carbocyclic substituents were not provided by the analysis, the unfavorable effect on dehydrogenation from hydrophilic and large substituents suggests that the active site of the mALDH is relatively rigid and that the orientation of the substrate in relation to the catalytic cysteine and the cofactor binding site is critical.

Carboxylic acid derivatives

Carboxylic acid derivatives of the formula: STR1 are provided, which are useful for treatment of androgen dependent diseases.