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DNA-dependent protein kinase catalytic subunit (DNA-PKcs) is a member of the PI3K-related kinase (PIKK) family.1,2,3 It is composed of an N-terminal domain, which consists of two domains of HEAT repeats, a FAT homology domain, a FKBP12-rapamycin-binding (FRB) domain, a kinase domain, a PIKK regulatory domain, and a C-terminal FAT domain (FATC). DNA-PKcs localizes to the nucleus, cytoplasm, plasma membrane, cytoskeleton, and lipid rafts.2,4 It is involved in DNA double-strand break (DSB) repair through non-homologous end-joining (NHEJ) and homologous recombination (HR) pathways and contains numerous phosphorylation sites that modify its activity, such as Ser2056, which must be autophosphorylated for NHEJ to occur in response to DSBs.1,2,3 DNA-PKcs also plays a role in mitosis, telomere maintenance, transcriptional regulation, innate and adaptive immunity, and senescence, among many other processes. DNA-PKcs interacts with Ku70/Ku80 to form the DNA-PK holoenzyme, which acts on various substrates, including histone H2AX, heat shock protein 90 (Hsp90), and Artemis.2,3 High expression or increased activity of DNA-PKcs is associated with metastasis, poor prognosis, and radio- and chemoresistance in various cancers.2 Cayman’s DNA-PKcs (Phospho-Ser2056) Rabbit Monoclonal Antibody (Clone RM500) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.
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3. The multifaceted functions of DNA-
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