Date published: 2026-1-7

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A cyclase V Inhibitors

Santa Cruz Biotechnology now offers a broad range of A cyclase V Inhibitors for use in various applications. A cyclase V inhibitors are specialized compounds designed to inhibit the activity of adenylyl cyclase type V, an enzyme responsible for the conversion of ATP to cyclic AMP (cAMP). cAMP serves as a crucial secondary messenger in various cellular processes, including metabolism, gene expression, and signal transduction. In scientific research, A cyclase V inhibitors are essential tools for exploring the regulation of cAMP pathways and their broader biological implications. Researchers use these inhibitors to study the modulation of cellular responses to hormonal signals, the impact on energy balance, and the role of cAMP in various physiological processes. By selectively inhibiting adenylyl cyclase V, scientists can dissect the specific contributions of this enzyme to cellular function and investigate the mechanisms underlying cAMP-mediated signaling pathways. These inhibitors are particularly valuable for understanding the nuances of signal transduction and the dynamic regulation of cellular activities. The availability of high-purity A cyclase V inhibitors from Santa Cruz Biotechnology ensures that experiments are conducted with precision and reproducibility, yielding reliable data that advance our understanding of cAMP-dependent processes. By providing a comprehensive selection of these inhibitors, Santa Cruz Biotechnology supports the scientific community in developing new experimental models and uncovering novel insights into cellular signaling and regulation. View detailed information on our available A cyclase V Inhibitors by clicking on the product name.

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Adenylyl Cyclase Type V Inhibitor, NKY80

299442-43-6sc-221217
sc-221217A
5 mg
25 mg
$124.00
$431.00
(0)

Adenylyl Cyclase Type V Inhibitor, NKY80, selectively targets adenylate cyclase V, exhibiting a high specificity for its active site. This compound disrupts the enzyme's catalytic function by stabilizing an inactive conformation, effectively reducing cyclic AMP production. Its unique interaction profile suggests a potential for allosteric modulation, influencing downstream signaling pathways. The inhibitor's kinetics indicate a reversible binding mechanism, highlighting its role in fine-tuning cellular responses.