The AIMP1 Knockout HAP1 Polyclonal Cells consist of a CRISPR/Cas9-edited polyclonal knockout cell population designed to disrupt the AIMP1 gene in the HAP1 human near-haploid cell line. This product provides a loss-of-function model for investigating the dual roles of AIMP1 in protein translation and extracellular inflammatory signaling. The polyclonal nature of the knockout population reflects a heterogeneous mixture of edited cells, enabling robust assessment of gene function without relying on single-cell-derived clonal expansion.
HAP1 cells originate from a male patient with chronic myelogenous leukemia and exhibit a predominantly haploid karyotype, with a fibroblast-like adherent morphology. Their near-haploid genomic content simplifies gene-editing efficiency and functional interpretation by reducing confounding alleles, making this cell line a widely accepted platform for genetic knockout studies. The HAP1 background supports consistent growth characteristics and is compatible with standard culture and transfection protocols, facilitating integration into diverse experimental workflows.
AIMP1 encodes p43, a scaffolding component of the multi-tRNA synthetase complex that facilitates aminoacylation and efficient translation. Proteolytic cleavage by stress-induced caspases or elastase generates the extracellular cytokine EMAP-II, which activates endothelial apoptosis, neutrophil chemotaxis, and macrophage activation while inhibiting VEGF-driven angiogenesis. Upstream regulators include TNF-??, interferons, and cellular stress signals such as hypoxia and serum starvation. AIMP1/p43 interacts with aminoacyl-tRNA synthetases like EPRS, KARS, and LARS, as well as with p18 (AIMP3), within the multisynthetase complex, linking translation to inflammatory pathways through TNF receptor-mediated NF-??B and caspase cascades.
In the HAP1 background, disruption of AIMP1 permits dissection of its translation-dependent and translation-independent functions without the compensatory effects of a diploid genome. Researchers can examine how loss of AIMP1 impacts global translation rates, multisynthetase complex integrity, and processing into EMAP-II. The model also enables the study of cytokine-mediated crosstalk between endothelial apoptosis and angiogenic suppression in a simplified genetic context, providing clarity for mechanistic studies often confounded by redundant gene copies.
Typical applications include western blotting and RT-qPCR to verify AIMP1/EMAP-II expression changes, immunofluorescence for subcellular localization of synthetase complex components, and co-immunoprecipitation to probe protein?Cprotein interactions. Functional assays may involve cytokine release measurements, endothelial cell apoptosis induction, tube formation assays to assess angiogenic responses, and proteolytic cleavage analysis using recombinant proteases. This knockout model is suited for oncology research, chronic inflammatory disease studies, and anti-angiogenic drug screening. For further details or technical inquiries, please contact Ascent Research.
