Alcohol Dehydrogenase Detection Kit

• Cat.No.: Kit-0052
• Product Overview: Alcohol Dehydrogenase Detection Kit provides a convenient tool for sensitive detection of the Alcohol DH in a variety of samples. In the assay Alcohol DH will utilize isopropanol as a substrate leading to a proportional color development. The activity of ADH can be easily quantified colorimetrically (? = 450 nm). This assay detects ADH activity as low as 0.01 mU in samples.

Specification

• Applications: Functional Studies
• Storage: Store the kit at -20°C, protect from light. Allow ADH Assay Buffer to warm to room temperature before use. Briefly centrifuge vials prior to opening. Read the entire protocol before performing the assay.DEVELOPER: Reconstitute Developer with 0.9 ml of ddH2O. Pipette up and down several times to completely dissolve the pellet into solution. (Do not vortex).

Reviews

01/08/2021

Demonstrates high sensitivity in detecting low abundance proteins in complex samples.

06/18/2020

Displays excellent membrane permeability in cell-penetrating peptide assays.

Q&As

Are there any known genetic variations or polymorphisms in the ADH gene associated with alcohol metabolism or susceptibility to alcohol-related disorders?

Genetic variations or polymorphisms in the ADH gene have been associated with differences in alcohol metabolism and susceptibility to alcohol-related disorders, linking genotype to phenotype.

What is the tissue-specific expression pattern of ADH, and are there any differences in its expression levels or isoform distribution across different organs or cell types?

ADH exhibits a tissue-specific expression pattern, with variations in expression levels and isoform distribution among different organs and cell types, reflecting its functional diversity.

How is the expression of ADH regulated under normal physiological conditions and in response to alcohol exposure or other metabolic factors?

The expression of ADH is regulated under normal physiological conditions, and it can be induced or suppressed in response to alcohol exposure or other metabolic factors, highlighting its adaptive nature.

What are the structural features and conformational changes of ADH upon substrate binding, and how do they influence enzymatic activity?

The structural features and conformational changes of ADH upon substrate binding play a crucial role in its enzymatic activity, influencing the efficiency and specificity of alcohol metabolism.

Can pharmacological agents or environmental factors modulate ADH expression or activity, and what are the potential implications for alcohol metabolism or therapy?

Pharmacological agents or environmental factors can modulate ADH expression or activity, potentially affecting alcohol metabolism and offering avenues for therapeutic interventions or personalized medicine.

What are the kinetic properties of different ADH isoforms, including their substrate specificity, affinity, and catalytic efficiency?

Different ADH isoforms display distinct kinetic properties, including substrate specificity, affinity, and catalytic efficiency, enabling them to metabolize alcohol and related substrates with varying efficiencies.

Can ADH catalyze the oxidation or reduction of other substrates apart from alcohol, and what are the implications for its broader metabolic role?

ADH can catalyze the oxidation or reduction of various substrates beyond alcohol, suggesting its involvement in broader metabolic pathways and potential metabolic interplay.

How does ADH activity or expression vary in individuals with different levels of alcohol consumption or in populations with varying alcohol-related cultural practices?

ADH activity or expression can vary among individuals with different levels of alcohol consumption and in populations with distinct alcohol-related cultural practices, reflecting the interplay between genetic and environmental factors.

How does ADH contribute to the overall metabolism and detoxification of alcohol, and what are the consequences of ADH deficiency or dysfunction?

ADH plays a central role in the overall metabolism and detoxification of alcohol, contributing to the conversion of alcohol to acetaldehyde and subsequently to acetic acid, with ADH deficiency or dysfunction leading to altered alcohol metabolism and potential susceptibility to alcohol-related pathologies.

Are there any cofactors or coenzymes required for ADH activity, and what is their role in modulating enzyme function or regulation?

ADH requires specific cofactors or coenzymes, such as NAD+ or NADH, for its activity, serving as electron carriers and regulators of ADH function.