Date published: 2026-5-13

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MTAP Substrates

Santa Cruz Biotechnology now offers a broad range of MTAP Substrates for use in various applications. Methylthioadenosine phosphorylase (MTAP) is an enzyme that plays a crucial role in the methionine salvage pathway, which is responsible for recycling methionine from 5'-methylthioadenosine (MTA), a byproduct of polyamine synthesis. This pathway is vital for maintaining cellular methionine levels, which are essential for various biological processes, including protein synthesis, methylation reactions, and polyamine production. MTAP Substrates are critical tools in scientific research, allowing researchers to study the enzymatic activity of MTAP and its impact on cellular metabolism and gene regulation. By utilizing these substrates, scientists can investigate how MTAP activity influences the methionine salvage pathway, providing insights into the enzyme's role in normal cellular function and its implications in diseases such as cancer, where MTAP deficiency is often observed. These substrates are widely used in biochemical assays to measure MTAP activity, in studies exploring the metabolic consequences of MTAP loss, and in research aimed at developing targeted therapies that exploit MTAP deficiency in cancer cells. The availability of these substrates has significantly advanced research in the fields of cancer biology, metabolic regulation, and enzymology, offering essential tools for understanding the complex interactions between metabolism and cellular function. View detailed information on our available MTAP Substrates by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

5′-Deoxy-5′-methylthioadenosine

2457-80-9sc-202427
50 mg
$122.00
1
(1)

5′-Deoxy-5′-methylthioadenosine acts as a potent inhibitor of the enzyme methylthioadenosine phosphorylase (MTAP), engaging in specific interactions that disrupt the enzyme's catalytic activity. Its unique sulfur-containing moiety enhances binding affinity, leading to altered metabolic flux in the salvage pathway of adenine. The compound's structural characteristics influence its stability and reactivity, impacting cellular energy dynamics and nucleotide synthesis.