The HSPA1L Knockout HAP1 Polyclonal Cells represent a CRISPR/Cas9-edited polyclonal knockout population targeting the HSPA1L gene in the human HAP1 near-haploid cell line. This product provides a mixed population of edited cells with loss-of-function mutations in HSPA1L, enabling robust functional genomics studies without the clonal selection step. The polyclonal format preserves genetic heterogeneity while disrupting the target gene, suitable for assays where population-level effects are analyzed.
HAP1 is a near-haploid cell line derived from the chronic myeloid leukemia (CML) cell line KBM-7. Its haploid karyotype greatly simplifies genetic analyses by reducing gene copy number, thereby facilitating the study of recessive phenotypes and loss-of-function mutations. HAP1 cells retain many characteristics of the myeloid lineage and are widely used as a model system for kinase signaling, drug sensitivity screens, and protein?Cprotein interaction studies.
HSPA1L encodes a stress-inducible member of the heat shock protein 70 (HSP70) family that functions as an ATP-dependent molecular chaperone. Under basal conditions, HSPA1L participates in protein folding, translocation, and degradation, while stress conditions such as heat shock or oxidative stress strongly upregulate its expression via the transcription factor HSF1. Mechanistically, HSPA1L interacts with co-chaperones including DNAJ/HSP40 proteins, HOP (STIP1), and BAG3 to facilitate client protein maturation and prevent aggregation. Notably, HSPA1L also modulates apoptosis through direct interactions with Bcl-2 family proteins, contributing to cell survival signaling, and has been linked to the MAPK pathway via JNK.
In the HAP1 background, disruption of HSPA1L generates a powerful model to investigate the role of stress-induced chaperone function in leukemia and other cellular contexts. The near-haploid nature of the host cells combined with polyclonal knockout enables efficient assessment of gene function in protein homeostasis, apoptotic regulation, and signaling crosstalk. Because HSPA1L contributes to the cellular stress response and drug resistance, this model is particularly valuable for examining how loss of the chaperone affects sensitivity to chemotherapeutic agents or proteotoxic stress.
Researchers can employ these HSPA1L polyclonal knockout cells in a variety of applications, including protein homeostasis studies under proteotoxic stress, analysis of heat shock response dynamics via RT-qPCR of HSF1 target genes, and apoptosis assays using Annexin V staining following stress induction. Co-immunoprecipitation experiments can probe altered chaperone?Cclient interactions, while cell viability assays under oxidative or chemotherapeutic stress dissect the contribution of HSPA1L to drug resistance. These cells also serve as a model for studying neuroprotective mechanisms and ischemia-reperfusion injury pathways. For additional information or to request custom services, please contact Ascent Research.
