In Stock Cell Lines
The NQO1 Knockout H1299 Cell Line is a CRISPR/Cas9-edited knockout cell line derived from the p53-null, KRAS G12S-mutant H1299 lung adenocarcinoma model. Loss of NQO1 disrupts the two-electron reduction of quinones, a key detoxification step regulated by NRF2 and KEAP1, and eliminates p53 stabilization functions. This model enables dissection of NQO1??s p53-independent roles in oxidative stress, ferroptosis, and chemoresistance to quinone-based drugs such as mitomycin C and beta-lapachone. It is suitable for NRF2 pathway analysis, ROS measurement, and drug sensitivity assays.
CARNMT1 Knockout Hela Polyclonal Cells
Cat. No. ARG23972
MACF1 Knockout NCI-H1975 Polyclonal Cells
Cat. No. ARG16935
MICU1 Knockout Hela Polyclonal Cells
Cat. No. ARG9026
BRPF3 Knockout Hela Polyclonal Cells
Cat. No. ARG23499
ADIPOR1 Knockout NCI-H1299 Polyclonal Cells
Cat. No. ARG30242
NAIF1 Knockout HEK293T Polyclonal Cells
Cat. No. ARG3618
The NQO1 Knockout H1299 Cell Line is a CRISPR/Cas9-edited knockout cell line derived from H1299 human non-small cell lung cancer cells. This loss-of-function model abrogates NQO1 expression, providing a stable platform to investigate NQO1-dependent processes. The gene disruption is mediated by CRISPR/Cas9 targeting, eliminating NQO1 enzymatic activity.
H1299 is a lung adenocarcinoma epithelial line established from a lymph node metastasis. It carries a homozygous TP53 deletion (p53-null) and an oncogenic KRAS G12S mutation, reflecting a common and aggressive genetic profile. The p53 deficiency uncouples NQO1 function from its canonical stabilization of p53, allowing dissection of p53-independent roles. H1299 exhibits robust proliferation and resistance to apoptosis, making it a relevant model for chemoresistance and redox stress studies.
NQO1 encodes a cytosolic flavoprotein that performs two-electron reduction of quinones to hydroquinones, preventing redox cycling and oxidative damage. Transcription is primarily induced by NRF2 via the antioxidant response element (ARE), with negative control by KEAP1; additional regulators include AhR, beta-naphthoflavone, and sulforaphane. Mechanistically, NQO1 forms complexes with p53, HSP90, and the 20S proteasome to hinder p53 degradation, though this function is moot in H1299. NQO1 also activates prodrugs like mitomycin C and beta-lapachone. Core pathway components include KEAP1, NRF2, HO-1, GST, and NQO1 itself.
In H1299 cells, NQO1 disruption eliminates a key node of the NRF2-driven antioxidant network. Combined with mutant KRAS, this knockout heightens sensitivity to oxidative stressors and ferroptosis inducers. It enables interrogation of NQO1??s metabolic contributions, including its role in bioactivating quinone-based chemotherapeutics. The model is particularly useful for studying compensatory pathways that sustain redox balance upon loss of NQO1, and for testing therapeutic strategies that exploit NQO1 deficiencies in p53-null lung cancers.
Applications include western blot and RT-qPCR for confirmation of NQO1 loss; enzymatic activity assays; ROS quantification; and viability assays with mitomycin C or beta-lapachone. NRF2 target gene panels and ferroptosis readouts can be implemented. This cell line supports research on oxidative stress signaling, xenobiotic metabolism, and p53-independent chemoresistance mechanisms. Contact Ascent Research for more information.
