The DTD1 Knockout NCI-H1975 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population derived from the NCI-H1975 human lung adenocarcinoma cell line. This product features CRISPR/Cas9-mediated disruption of DTD1, generating a heterogeneous pool of edited cells. The polyclonal format provides a robust loss-of-function model without clonal selection, preserving genetic diversity for functional studies.
NCI-H1975 is a non-small cell lung cancer (NSCLC) cell line established from the pleural effusion of a female patient with lung adenocarcinoma. It harbors EGFR L858R and T790M mutations, making it a key model for studying EGFR-targeted therapies and drug resistance mechanisms in NSCLC.
DTD1 encodes D-tyrosyl-tRNA deacylase, which hydrolyzes mischarged D-tyrosyl-tRNA(Tyr) to prevent D-tyrosine incorporation into nascent proteins. This enzyme interacts with tyrosyl-tRNA synthetase (YARS) and elongation factor 1A (eEF1A) and functions within ribosomal translation complexes. Loss of DTD1 disrupts translational quality control, leading to accumulation of D-amino acid-containing proteins that may overwhelm the proteasome and impair proteostasis. Although upstream regulation is not well characterized, DTD1 activity is potentially linked to cellular stress pathways.
In NCI-H1975 cells, DTD1 knockout is expected to elevate D-amino acid incorporation, exacerbating proteotoxic stress and altering signaling under oncogenic EGFR activity. The polyclonal population enables investigation of translational fidelity defects in a therapeutically relevant NSCLC genetic background, avoiding clonal biases.
These cells support diverse applications including Western blotting and RT-qPCR for knockout confirmation, cell viability and clonogenic survival assays, proteostasis reporter assays, and mass spectrometry-based D-amino acid detection. They are ideal for studying translational fidelity in cancer, D-amino acid toxicity, tRNA editing enzyme function, and drug target validation in NSCLC. For further inquiries, please contact Ascent Research.
