The HSPH1 Knockout HAP1 Polyclonal Cells represent a CRISPR/Cas9-edited polyclonal knockout cell population engineered to disrupt the HSPH1 gene within the near-haploid HAP1 cell line. This polyclonal pool provides a heterogeneous loss-of-function model that enables investigation of HSPH1-dependent mechanisms without clonal selection artifacts. The product is supplied as a ready-to-use cell population for downstream functional assays, offering a robust tool for studying the nucleotide exchange factor activity, chaperone function, and anti-apoptotic roles of HSPH1 in a simplified genomic context.
The host HAP1 cell line is a suspension-adapted human cell line derived from the KBM-7 chronic myeloid leukemia (CML) background. It is characterized by a near-haploid karyotype, making it particularly valuable for genetic screening and loss-of-function studies. The haploid state facilitates unambiguous genotype?Cphenotype correlations, as the disruption of a single allele directly manifests in the cellular phenotype. HAP1 cells are well-established in biomedical research for their ease of culture, stable growth, and compatibility with high-throughput screening formats, supporting a wide range of applications from signaling dissection to drug discovery.
HSPH1 (heat shock protein family H (Hsp110) member 1) functions as a nucleotide exchange factor for HSP70, catalyzing ADP/ATP exchange to enhance substrate binding and release cycles, thereby accelerating chaperone activity. Under stress conditions such as heat shock, oxidative stress, or inflammatory cytokine exposure (TNF-??, IL-6), HSF1 transcriptionally upregulates HSPH1. HSPH1 interacts with HSP70, HSP40, Bcl-2 family proteins, Apaf-1, and the ubiquitin ligase CHIP to coordinate protein folding quality control and apoptosis regulation. Specifically, HSPH1 inhibits apoptosis by interacting with Bax and Apaf-1, preventing caspase activation, while also modulating JNK signaling. This integrative network involves representative pathway components including HSF1, HSP70, HSP40, HSP90, Bcl-2, and caspases.
In the HAP1 near-haploid background, HSPH1 knockout is expected to sensitize cells to proteotoxic stress and alter apoptotic thresholds, providing a clean genetic system to dissect the chaperone??s cytoprotective functions. The model is particularly suited to investigate how loss of HSPH1 impacts client protein folding, HSP70 ATPase cycle dynamics, and stress-induced apoptosis. Given the relevance of HSPH1 to cancer progression (colorectal, breast, esophageal), neurodegenerative protein aggregation disorders, and ischemia-reperfusion injury, this knockout pool enables researchers to explore the molecular basis of these pathologies and to identify synthetic lethal interactions or compensatory mechanisms.
This product supports diverse research applications including cancer biology, cellular stress response elucidation, chaperone network analysis, and apoptosis pathway investigation. Representative assays include western blotting and RT-qPCR for expression profiling, immunofluorescence for subcellular localization, co-immunoprecipitation to assess HSPH1?CHSP70 interaction, ATPase activity measurements to evaluate chaperone cycle effects, flow cytometry for apoptosis quantification (e.g., Annexin V staining), and cell viability assays under heat shock or oxidative stress. For additional technical specifications, validation data, or pricing inquiries, please contact Ascent Research.
