Date published: 2026-4-24

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PKD Inhibitors

Santa Cruz Biotechnology now offers a broad range of PKD inhibitors for use in various applications. PKD inhibitors are a crucial category of chemical compounds that selectively inhibit protein kinase D (PKD) enzymes, which are vital in regulating numerous cellular processes, including signal transduction, gene expression, and cell proliferation. In scientific research, these inhibitors are extensively utilized to study the functional roles of PKD isoforms in cellular signaling pathways. By selectively targeting PKD activity, researchers can dissect the complex networks involved in cell growth, differentiation, and survival. This allows for a deeper understanding of the mechanisms underlying cellular responses to external stimuli and the modulation of various intracellular processes. Furthermore, PKD inhibitors are valuable tools in investigating the molecular basis of diseases associated with aberrant PKD signaling. The ability to modulate PKD activity with precision makes these inhibitors indispensable in the study of biochemical pathways, aiding in the development of novel scientific strategies and the advancement of knowledge in cellular biology. View detailed information on our available PKD inhibitors by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Calphostin C

121263-19-2sc-3545
sc-3545A
100 µg
1 mg
$343.00
$1642.00
20
(1)

Calphostin C is a potent inhibitor of protein kinase C (PKC), characterized by its ability to selectively bind to the regulatory domain of the enzyme. This interaction disrupts the phosphorylation cascade, altering signal transduction pathways. Its unique structure allows for specific conformational changes in PKC, influencing enzyme activity and substrate recognition. The compound's kinetic profile reveals a competitive inhibition mechanism, providing insights into the modulation of cellular signaling dynamics.

Resveratrol

501-36-0sc-200808
sc-200808A
sc-200808B
100 mg
500 mg
5 g
$80.00
$220.00
$460.00
64
(2)

Resveratrol acts as a potent modulator of protein kinase D (PKD) through its ability to interact with specific phosphorylation sites, influencing the enzyme's activity. Its unique polyphenolic structure facilitates hydrogen bonding and hydrophobic interactions, enhancing selectivity for PKD. This compound exhibits a distinct kinetic behavior, demonstrating non-competitive inhibition, which alters the enzyme's conformational dynamics and impacts downstream signaling pathways.

CID 755673

521937-07-5sc-205246
10 mg
$203.00
1
(1)

CID 755673 functions as a selective inhibitor of protein kinase D (PKD) by engaging in specific molecular interactions that stabilize its inactive conformation. Its unique structural features allow for effective binding at the enzyme's active site, disrupting substrate access. The compound exhibits a rapid association and slower dissociation rate, leading to prolonged inhibition. Additionally, its ability to form stable complexes with PKD enhances its specificity, influencing cellular signaling cascades.

TGF-β RI Kinase Inhibitor V

627536-09-8sc-203294
2 mg
$88.00
3
(1)

TGF-β RI Kinase Inhibitor V acts as a potent modulator of protein kinase D (PKD) through its unique ability to disrupt the phosphorylation cascade. By selectively targeting the ATP-binding pocket, it alters the enzyme's conformational dynamics, preventing substrate phosphorylation. The compound's distinct binding affinity results in a notable alteration of downstream signaling pathways, showcasing its role in fine-tuning cellular responses. Its kinetic profile reveals a fast onset of action, contributing to sustained inhibition.

Gossypol

303-45-7sc-200501
sc-200501A
25 mg
100 mg
$116.00
$230.00
12
(1)

Gossypol exhibits intriguing interactions with protein kinase D (PKD) by acting as a competitive inhibitor, effectively blocking substrate access to the active site. Its unique structural features allow for specific hydrogen bonding and hydrophobic interactions, enhancing binding affinity. This compound influences the allosteric regulation of PKD, leading to altered enzymatic activity and modulation of cellular signaling networks. The reaction kinetics indicate a gradual onset, suggesting prolonged effects on PKD activity.