DPP7 Knockout HAP1 Polyclonal Cells are a CRISPR/Cas9 gene disruption pool in the near-haploid HAP1 cell line, providing loss of DPP7 dipeptidyl peptidase function. The polyclonal format avoids clonal selection artifacts and maintains genetic heterogeneity, suitable for population-based assays in proteolysis and cancer research. These cells enable investigation of intracellular peptide turnover and related signaling without requiring single-cell cloning.
HAP1 cells are a male-derived near-haploid chronic myeloid leukemia (CML) line with a stable haploid complement in a substantial fraction of the population. This unusual karyotype simplifies CRISPR/Cas9 knockout generation because most genes exist as single copies, reducing the need for biallelic targeting. HAP1 cells retain key cancer signaling features and are widely used in haploid genetic screens, drug target identification, and cancer model studies. Their CML origin provides a context for examining protease-dependent regulation of cell quiescence and metabolic adaptation, processes frequently dysregulated in leukemia.
DPP7 encodes a cytoplasmic serine protease that exhibits proline-specific dipeptidyl peptidase activity, cleaving N-terminal dipeptides from polypeptide substrates and contributing to intracellular peptide turnover and amino acid recycling. Its expression is regulated by TP53 and FOXO transcription factors under nutrient deprivation, and it functions downstream of the proteasome to process peptide fragments. DPP7 directly influences the levels of proline-containing dipeptides and free amino acids, which in turn modulate mTORC1 signaling, a key regulator of cell growth and quiescence. Within the proteolytic network, DPP7 interacts with substrate peptides and proteasome components such as proteasome subunit beta type-5, alongside related peptidases including DPP4, PREP, and cathepsin B. Disruption of DPP7 therefore alters peptide homeostasis and quiescence signals.
In HAP1 cells, DPP7 knockout allows dissection of cytoplasmic dipeptidase activity in cancer quiescence. As a CML line, HAP1 relies on precise metabolic control; loss of DPP7 may alter peptide recycling and amino acid availability, affecting mTORC1 signaling. This model helps reveal how proteolytic processing maintains quiescence in leukemia, a therapy-resistant state. The near-haploid background also facilitates combinatorial knockout and genome-wide screens for DPP7 interactors.
These DPP7-knockout polyclonal cells suit functional studies of proteolysis in cancer, intracellular peptide analysis via proteomics or amino acid profiling, and dipeptidyl peptidase inhibitor screening. Applications include quiescence assays under nutrient deprivation, proliferation assays, and signaling validation by western blot or RT-qPCR. The polyclonal format supports population-level biochemical experiments. For product details or custom services, contact Ascent Research.
