Date published: 2026-2-1

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DNA-PK Inhibitors

Santa Cruz Biotechnology now offers a broad range of DNA-PK Inhibitors for use in various applications. DNA-dependent protein kinase (DNA-PK) is a critical enzyme involved in the repair of DNA double-strand breaks through the non-homologous end joining (NHEJ) pathway, a key mechanism for maintaining genomic stability. DNA-PK Inhibitors are essential tools in scientific research, allowing researchers to explore the role of DNA-PK in DNA repair processes and how its inhibition affects cellular responses to DNA damage. By inhibiting DNA-PK, scientists can study the impact on DNA repair efficiency, genomic integrity, and the activation of DNA damage response pathways, providing valuable insights into how cells maintain their genetic material under stress. These inhibitors are widely used in studies focused on understanding the molecular mechanisms of DNA repair, particularly in the context of how cells manage and respond to DNA double-strand breaks. Additionally, DNA-PK Inhibitors are valuable for investigating the interplay between different DNA repair pathways and the potential consequences of inhibiting key repair enzymes on cellular survival and genome stability. The availability of these inhibitors has significantly advanced research in fields such as molecular biology, genetics, and cancer research, offering critical tools for dissecting the complex processes that ensure accurate DNA repair and the maintenance of genomic stability. View detailed information on our available DNA-PK Inhibitors by clicking on the product name.

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

XL-147 derivative 1

1349796-36-6sc-364660
sc-364660A
5 mg
50 mg
$189.00
$1725.00
(0)

XL-147 derivative 1 functions as a DNA-PK inhibitor, distinguished by its ability to disrupt the enzyme's structural integrity through targeted hydrophobic interactions. This compound selectively modulates the enzyme's active site, preventing substrate binding and subsequent phosphorylation events. Its unique reaction kinetics reveal a rapid initial binding phase, followed by a slower dissociation, providing insights into the dynamic regulation of DNA repair mechanisms. The compound's specificity highlights its potential to elucidate the intricate pathways involved in cellular responses to DNA damage.