Date published: 2025-10-19

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ALDH1A1 Substrates

Santa Cruz Biotechnology now offers a broad range of ALDH1A1 Substrates for use in various applications. ALDH1A1 Substrates are critical in scientific research for investigating the role of the aldehyde dehydrogenase 1 family, member A1 (ALDH1A1) enzyme in the metabolism of aldehydes. ALDH1A1 is a key enzyme responsible for converting retinaldehyde to retinoic acid, a vital molecule in cellular differentiation, development, and homeostasis. By utilizing specific substrates, researchers can monitor ALDH1A1 activity and study its contribution to crucial biological processes. These substrates are particularly important in research exploring the role of ALDH1A1 in maintaining stem cell properties, as this enzyme is often associated with the stemness and self-renewal capabilities of various cell types. In addition, ALDH1A1 Substrates are valuable tools for examining the enzyme's involvement in detoxifying harmful aldehydes, thereby protecting cells from oxidative stress and contributing to cellular resilience. In the scientific community, ALDH1A1 Substrates are widely used in studies focused on understanding metabolic pathways, enzyme kinetics, and the enzyme's role in disease progression, particularly in cancer research, where ALDH1A1 is often implicated in tumor initiation and resistance to therapy. Researchers use these substrates in various experimental models, including in vitro assays and in vivo studies, to gain insights into the biochemical and molecular functions of ALDH1A1. The availability of high-quality ALDH1A1 Substrates is essential for advancing research in areas such as cell biology, developmental biology and molecular biology, offering the tools needed to explore enzyme activity and its impact on cellular function. View detailed information on our available ALDH1A1 Substrates by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Resorufin acetate

1152-14-3sc-208300
25 mg
$194.00
(1)

Resorufin acetate serves as a fluorescent probe, demonstrating unique interactions with aldehyde dehydrogenase 1A1 (ALDH1A1) through its electrophilic nature. The compound undergoes hydrolysis, releasing resorufin, which exhibits a distinct red fluorescence. This transformation is influenced by the enzyme's active site, promoting specific binding and catalysis. The reaction kinetics reveal a notable sensitivity to pH and temperature, affecting the rate of conversion and fluorescence intensity, thereby providing insights into enzyme activity and cellular metabolism.