Date published: 2025-10-15

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Creatine Kinase Substrates

Santa Cruz Biotechnology now offers a broad range of Creatine Kinase Substrates for use in various applications. Creatine kinase (CK) is a critical enzyme that plays a vital role in energy metabolism by catalyzing the conversion of creatine and ATP into phosphocreatine and ADP, a process essential for maintaining cellular energy homeostasis, particularly in tissues with high energy demands like muscle and brain. Creatine Kinase Substrates are indispensable tools in scientific research for studying the enzymatic activity and regulation of CK, providing insights into its role in cellular energy transfer and its involvement in various metabolic pathways. Researchers utilize these substrates to explore how CK contributes to the rapid regeneration of ATP, especially during periods of intense energy usage, and how alterations in CK activity can affect cellular and tissue function. These substrates are widely used in biochemical assays to measure CK activity, enabling the detailed analysis of its kinetic properties, substrate specificity, and the factors that regulate its activity under different physiological conditions. In addition, Creatine Kinase Substrates are employed in studies investigating the enzyme's role in muscle physiology, bioenergetics, and the broader implications of CK function in health and disease. The availability of these substrates has significantly advanced research in fields such as biochemistry, physiology, and sports science, offering critical tools for understanding the molecular mechanisms of energy metabolism and the role of CK in maintaining cellular energy balance. View detailed information on our available Creatine Kinase Substrates by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Sodium creatine phosphate dibasic tetrahydrate

922-32-7sc-208394
sc-208394A
1 g
5 g
$61.00
$94.00
(1)

Sodium creatine phosphate dibasic tetrahydrate acts as a crucial energy reservoir, facilitating the rapid regeneration of ATP through its interaction with creatine kinase. Its unique structural conformation allows for efficient binding to the enzyme, enhancing reaction kinetics and promoting effective substrate channeling. The compound's solubility and stability in aqueous environments support its role in cellular energy transfer, influencing metabolic flux and energy homeostasis in various biological systems.