Date published: 2025-12-1

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NOS1 Substrates

Santa Cruz Biotechnology now offers a broad range of NOS1 Substrates for use in various applications. NOS1 substrates, critical components in biochemical pathways, are indispensable in the study of nitric oxide synthase (NOS1) enzyme mechanisms. These substrates, typically amino acids or analogs, participate in the catalytic processes that facilitate the conversion of L-arginine to nitric oxide and citrulline, an essential reaction in cellular signaling and homeostasis. Research utilizing NOS1 substrates provides profound insights into enzymatic activity and regulation, helping to study the fundamental principles of enzyme kinetics and interaction. Scientists leverage these substrates to investigate the precise mechanisms of NOS1, facilitating advancements in our understanding of enzymatic behavior under various conditions. The availability of diverse NOS1 substrates enables researchers to conduct a wide array of experiments, from studying the binding affinity and specificity of the enzyme to exploring the effects of different substrate modifications on NOS1 activity. This research is pivotal in the broader context of biochemistry and molecular biology, where understanding enzyme-substrate interactions is crucial for developing innovative approaches to manipulate biochemical pathways. Moreover, the insights gained from studies involving NOS1 substrates contribute to the development of novel experimental techniques and tools, enhancing the precision and scope of biochemical research. View detailed information on our available NOS1 Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

N-Cyclopropyl-N′-hydroxyguanidine hydrochloride

551935-92-3sc-222000
sc-222000A
1 mg
5 mg
$30.00
$72.00
(0)

N-Cyclopropyl-N'-hydroxyguanidine hydrochloride exhibits unique interactions with NOS1, primarily through its ability to stabilize enzyme conformations via hydrophobic and electrostatic interactions. The cyclopropyl group introduces distinct steric hindrance, influencing substrate orientation and binding affinity. Additionally, the hydroxyl group enhances solubility and may facilitate intramolecular hydrogen bonding, potentially modulating reaction kinetics and altering the enzyme's catalytic efficiency in nitric oxide production.