The JMJD7 Knockout HAP1 Polyclonal Cells constitute a CRISPR/Cas9-edited polyclonal knockout cell population designed to abrogate JMJD7 gene function. This product utilizes a heterogeneous pool of HAP1 cells harboring targeted disruption of the JMJD7 locus, providing a loss-of-function model for studying JMJD7-dependent biology without clonal isolation. The polyclonal format preserves the genetic diversity inherent in the knockout pool, enabling robust population-level analyses of gene function while minimizing clonal artifacts. Researchers can employ these cells to interrogate the roles of JMJD7 in translational control, protein arginine hydroxylation, and cancer cell growth with high reproducibility.
Derived from the KBM-7 chronic myeloid leukemia cell line, HAP1 cells are a near-haploid, male, adherent cell line with a fibroblast-like morphology. They carry the Philadelphia chromosome, expressing the BCR-ABL1 oncogenic fusion kinase, which drives aberrant proliferation and survival signaling. The near-haploid karyotype facilitates unambiguous genetic manipulation, making HAP1 a favored model for functional genomics and CRISPR-based screens. This genetic tractability, combined with the leukemic background, renders HAP1 cells particularly suitable for dissecting gene functions relevant to myeloid malignancies and oncogenic signaling networks.
JMJD7 encodes a JmjC domain-containing protein that functions as a Fe2+/2-oxoglutarate-dependent arginine hydroxylase. Its primary characterized substrate is ribosomal protein S2 (RPS2), where it catalyzes C3 hydroxylation of specific arginine residues. This post-translational modification modulates ribosomal function and overall protein synthesis, linking JMJD7 activity to translation regulation and cell growth control. While the upstream regulators of JMJD7 remain poorly defined, its molecular interactions center on ribosomal proteins and cofactor binding. Downstream, JMJD7-mediated RPS2 hydroxylation influences translation initiation and elongation, thereby impacting cellular proliferation dynamics.
In the HAP1 context, JMJD7 knockout disrupts arginine hydroxylation on RPS2, potentially altering translation efficiency and growth characteristics. Given the BCR-ABL1-driven nature of HAP1 cells, which rely on heightened protein synthesis for survival, loss of JMJD7 may sensitize these cells to translational stress or modify oncogenic signaling outputs. Thus, this polyclonal knockout model offers a physiologically relevant system to explore the intersection of protein hydroxylation and leukemogenic pathways, aiding in the identification of vulnerabilities specific to cancer cells with dysregulated translation.
This product supports a wide range of research applications, including mechanistic studies of arginine hydroxylation and its impact on ribosome function. Representative assays include western blotting to assess JMJD7 protein levels and RPS2 hydroxylation status, RT-qPCR for downstream target expression, proliferation assays to quantify growth effects, polysome profiling to evaluate translation dynamics, co-immunoprecipitation for interaction studies, and mass spectrometry for direct detection of arginine hydroxylation. These tools enable in-depth functional genomics investigations in cancer biology, protein modification, and translational control. Researchers seeking further information or custom configurations are encouraged to contact Ascent Research.
