The HSP90AB1 Knockout SVG p12 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout population of human astrocytes, designed to disrupt the HSP90AB1 gene. Derived from the immortalized SVG p12 astrocyte cell line, this polyclonal pool provides a loss-of-function model for investigating chaperone-dependent proteostasis and signal transduction in a glial context, without clonal bias.
SVG p12 is an SV40 large T-antigen-immortalized human fetal astrocyte cell line that retains key features of primary astrocytes, including their role in providing structural and metabolic support to neurons, maintaining the blood-brain barrier, regulating neurotransmission, and responding to CNS injury. This well-characterized model ensures reproducible in vitro studies of astrocyte biology.
HSP90AB1 encodes the ATP-dependent molecular chaperone HSP90-beta, which facilitates folding and stabilization of client proteins involved in cell survival and proliferation. It is transcriptionally upregulated by HSF1 during cellular stress, and its activity depends on co-chaperones such as STIP1, CDC37, AHA1, and PTGES3. Key clients include kinases (RAF1, AKT1, CDK4), steroid hormone receptors, and transcription factors (HIF1A, NF-??B). Through these interactions, HSP90AB1 governs PI3K/AKT and MAPK/ERK signaling, and steroid receptor-mediated transcriptional programs. Gene disruption compromises client stability, leading to impaired growth factor responses, increased apoptosis, and sensitivity to proteotoxic stress.
In astrocyte biology, HSP90AB1 is critical for managing the high protein synthetic and stress-buffering demands of these glial cells. Disruption of this chaperone in SVG p12 cells provides a unique platform to study reactive astrogliosis, neuroinflammatory signaling, and the consequences of proteostatic failure observed in neurodegeneration and ischemia. The model also enables examination of how loss of HSP90 function may influence the malignant transformation of astrocytes, relevant to glioblastoma research.
Researchers can utilize these polyclonal cells for western blotting to assess stability of clients such as RAF1 and AKT, RT-qPCR analysis of stress-induced genes, and immunofluorescence to observe HSP90AB1 subcellular redistribution. Co-immunoprecipitation experiments can probe client?Cchaperone interactions, while MTT and apoptosis assays quantify cell viability. Phospho-flow cytometry for AKT and ERK activation, wound healing migration assays, and RNA-seq transcriptomic profiling are also applicable. This product is suited for validation of HSP90 inhibitors in oncology and neuroinflammation. For further information, contact Ascent Research.
