The Ahsa1 Knockout BV-2 Polyclonal Cells product consists of a CRISPR/Cas9-edited polyclonal knockout cell population derived from BV-2 mouse microglial cells, in which the Ahsa1 gene is disrupted to abolish expression of the AHA1 co-chaperone. This genetically diverse pool avoids clonal selection bias, providing a robust loss-of-function model for studying Ahsa1-dependent cellular processes in a microglial context. The cells are suitable for assays that probe Hsp90 chaperone function and downstream signaling.
The BV-2 cell line is an immortalized murine microglial model established from C57BL/6 mice, retaining key features of primary microglia such as phagocytic activity, inflammatory cytokine production, and responsiveness to immune stimuli. As resident immune cells of the central nervous system, BV-2 cells are extensively employed to investigate neuroinflammatory mechanisms and microglia-mediated clearance of protein aggregates, offering a physiologically relevant platform for mechanistic studies.
The AHA1 co-chaperone directly binds to Hsp90 (Hsp90aa1, Hsp90ab1) and stimulates its ATPase activity, accelerating the conformational cycle for client protein folding and activation. This function operates within a network including Hsp70 (Hspa1a), Hop (Stip1), p23 (Ptges3), and Cdc37. Transcriptional regulation by HSF1 under stress places AHA1 at the nexus of proteotoxic responses. Downstream, it promotes maturation of Hsp90 clients like protein kinases (Src, Akt, Raf-1, CDK4), steroid hormone receptors, and mutant p53, regulating signal transduction and stress adaptation.
In microglial cells, AHA1-mediated Hsp90 activity is likely involved in modulating neuroinflammatory signaling, as Hsp90 clients include kinases that feed into NF-??B and MAP kinase pathways. Loss of Ahsa1 may impair proper folding and clearance of aggregation-prone proteins such as tau or ??-synuclein, which are relevant to neurodegenerative diseases. Consequently, this knockout model enables the study of how co-chaperone dysfunction impacts microglial activation, phagocytosis, and the innate immune response within the central nervous system.
This product is suitable for investigating Hsp90 chaperone cycle mechanisms using ATPase activity assays, co-immunoprecipitation of AHA1-Hsp90 complexes, and western blotting for client proteins. It can be employed in Hsp90 inhibitor sensitivity testing (e.g., with 17-AAG), NF-??B luciferase reporter assays, RT-qPCR of stress genes, and immunofluorescence to track Hsp90 localization. Additional applications include flow cytometry for apoptosis, phagocytosis assays to measure functional microglial responses, and protein aggregation studies. For further details, please contact Ascent Research.
