HRP and AP Substrates

Naphthol AS-MX phosphate disodium salt serves as a versatile substrate for horseradish peroxidase (HRP) and alkaline phosphatase (AP), distinguished by its capacity for specific molecular interactions that enhance enzymatic efficiency. The compound's unique structural arrangement allows for optimal binding, promoting accelerated reaction kinetics. Its anionic phosphate moieties facilitate electrostatic interactions, influencing enzyme conformation and activity, thereby playing a crucial role in various biochemical processes.

5-Bromo-4-chloro-3-indoxyl phosphate, disodium salt, is a specialized substrate for horseradish peroxidase (HRP) and alkaline phosphatase (AP), characterized by its unique indoxyl structure that enables selective enzymatic cleavage. The compound exhibits distinct colorimetric properties upon enzymatic action, allowing for sensitive detection. Its halogenated aromatic system enhances hydrophobic interactions, influencing enzyme-substrate affinity and promoting efficient catalytic pathways in biochemical assays.

5-Bromo-6-chloro-3-indolyl phosphate, p-toluidine salt, serves as a distinctive substrate for horseradish peroxidase (HRP) and alkaline phosphatase (AP), featuring a unique indole framework that facilitates specific enzymatic interactions. The presence of halogen substituents modulates electronic properties, enhancing reactivity and selectivity in enzymatic pathways. Its solubility characteristics and hydrophobic nature contribute to improved enzyme binding, optimizing reaction kinetics in various biochemical applications.

5-Bromo-3-indoxyl phosphate, p-toluidine salt, is a specialized substrate for horseradish peroxidase (HRP) and alkaline phosphatase (AP), characterized by its indoxyl structure that promotes selective enzymatic recognition. The bromine substituent influences the compound's electronic distribution, enhancing its reactivity. Its unique steric properties and hydrophilic interactions facilitate efficient enzyme-substrate complexes, leading to accelerated reaction rates in biochemical assays.

6-Chloro-3-indoxyl phosphate, p-toluidine salt, serves as a distinctive substrate for horseradish peroxidase (HRP) and alkaline phosphatase (AP), featuring a chloro group that modulates its electronic characteristics and enhances enzymatic affinity. The compound's indoxyl framework allows for specific binding interactions, while its solubility profile supports rapid diffusion in aqueous environments. This substrate exhibits unique kinetic behavior, promoting efficient turnover in enzymatic reactions.

3-Indoxyl phosphate, bis(2-amino-2-methyl-1,3-propanediol) salt, acts as a specialized substrate for horseradish peroxidase (HRP) and alkaline phosphatase (AP), characterized by its dual amino alcohol structure that enhances solubility and stability. The compound's phosphate group facilitates specific enzymatic interactions, while its unique steric configuration influences reaction kinetics, allowing for optimized substrate conversion and efficient enzymatic activity in various biochemical pathways.

3-Indoxyl phosphate, disodium salt, serves as a versatile substrate for horseradish peroxidase (HRP) and alkaline phosphatase (AP), distinguished by its unique indole structure that promotes specific binding interactions. The presence of the phosphate moiety enhances its reactivity, enabling selective hydrolysis and oxidation processes. Its distinct electronic properties and steric arrangement contribute to tailored reaction kinetics, facilitating efficient enzyme-substrate complexes in diverse biochemical reactions.

3-Indoxyl phosphate p-toluidine salt is characterized by its unique indole framework, which facilitates specific interactions with enzymes like horseradish peroxidase (HRP) and alkaline phosphatase (AP). The p-toluidine component enhances solubility and stability, while the phosphate group allows for targeted enzymatic modifications. This compound exhibits distinct reactivity patterns, promoting rapid electron transfer and efficient catalytic cycles, making it a valuable tool in biochemical assays.

Naphthol AS-BI-phosphate, disodium salt, features a naphthol structure that enhances its affinity for enzyme active sites, particularly with horseradish peroxidase (HRP) and alkaline phosphatase (AP). The disodium salt form improves solubility in aqueous environments, facilitating swift diffusion and interaction. Its phosphate moiety enables specific phosphorylation reactions, while the naphthol ring contributes to unique electron-donating properties, promoting efficient redox processes in enzymatic assays.

Phenolphthalein monophosphate, bis(cyclohexylammonium) salt exhibits unique characteristics that enhance its reactivity with horseradish peroxidase (HRP) and alkaline phosphatase (AP). The cyclohexylammonium moieties provide steric bulk, influencing enzyme-substrate interactions and stabilizing the compound in solution. Its phenolphthalein structure allows for distinct colorimetric changes upon enzymatic action, facilitating real-time monitoring of reaction kinetics and enhancing assay sensitivity.