Date published: 2026-4-1

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SK Inhibitors

Santa Cruz Biotechnology now offers a broad range of SK Inhibitors for use in various applications. SK inhibitors, which target small-conductance calcium-activated potassium channels (SK channels), are critical tools in neurophysiological and cardiovascular research. These channels play a key role in afterhyperpolarization phases that follow action potentials in neurons, which are essential for regulating neuronal excitability and the fine-tuning of neuronal firing. By inhibiting SK channels, researchers can study the modulation of cellular excitability and synaptic plasticity, uncovering fundamental mechanisms that control neural rhythms and patterns associated with cognitive functions. In cardiovascular research, SK inhibitors help explore how these channels influence heart rate and myocardial contractility, offering insights into cardiac physiology. Beyond neuroscience and cardiology, SK inhibitors are employed in studying the cellular mechanisms underlying smooth muscle function and endothelial behavior, contributing to broader physiological insights. The manipulation of SK channels through these inhibitors provides a method to dissect the roles of these channels in various cell types and tissues without the influences of systemic biological processes, thereby enhancing the precision of experimental outcomes. SK inhibitors also serve as valuable tools in the development of new experimental models, particularly in the study of learning, memory, and behavior in animal models. Through the provision of these specialized compounds, Santa Cruz Biotechnology supports diverse scientific endeavors aimed at decoding complex biological interactions and functions. View detailed information on our available SK Inhibitors by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Apamin

24345-16-2sc-200994
sc-200994A
500 µg
1 mg
$171.00
$286.00
7
(1)

Apamin is a selective inhibitor of small-conductance calcium-activated potassium (SK) channels, exhibiting a unique affinity for specific channel subtypes. Its molecular interactions involve binding to the channel's intracellular domains, leading to altered gating properties. This compound demonstrates distinct reaction kinetics, characterized by a slow dissociation rate, which prolongs its inhibitory effects. Furthermore, apamin's structural features contribute to its stability in various environments, influencing its interaction dynamics with lipid membranes.