In Stock Cell Lines
Mus musculus (Mouse)
Lung
Adherent and suspension
The Hspb8 Knockout MH-S Cell Line is a CRISPR/Cas9-engineered murine alveolar macrophage model with targeted disruption of the Hspb8 gene, encoding a small heat shock protein critical for chaperone-assisted selective autophagy. HSPB8 cooperates with BAG3 and HSPA1A/heat shock protein 70 to facilitate degradation of misfolded proteins and inhibit apoptosis. This cell line enables analysis of autophagy, proteostasis, and innate immune function in a pulmonary context, with applications in protein aggregation research, neurodegeneration modeling, and drug screening. Standard assays include western blotting, LC3 turnover, and cytokine profiling.
IL1RN Knockout HAP1 Polyclonal Cells
Cat. No. ARG22770
KAT2A Knockout HEK293 Polyclonal Cells
Cat. No. ARG23241
HRAS Knockout CAL27 Polyclonal Cells
Cat. No. ARG35383
ALDH1B1 Knockout KYSE150 Polyclonal Cells
Cat. No. ARG36206
CUL4B Knockout HCT116 Polyclonal Cells
Cat. No. ARG7035
Prkdc Knockout CT26 Cell Line
Cat. No. ARG0205
The Hspb8 Knockout MH-S Cell Line is a CRISPR/Cas9-edited murine alveolar macrophage line bearing targeted disruption of the Hspb8 locus. It provides a stable loss-of-function model for investigating the small heat shock protein HSPB8 within a pulmonary immune cell context. As a defined genetic tool, this knockout cell line facilitates in-depth analysis of chaperone-assisted selective autophagy and stress-responsive pathways.
MH-S cells originate from BALB/c mouse bronchoalveolar lavage and represent an immortalized alveolar macrophage population. These cells execute essential pulmonary immune roles, including phagocytic clearance and cytokine release, and are commonly employed to study macrophage biology, host defense, and inflammatory responses. The BALB/c background ensures experimental reproducibility and is well suited for integration with other syngeneic models.
HSPB8 functions as a molecular chaperone that, through its incorporation into a complex with BAG3 and HSPA1A/heat shock protein 70, mediates selective autophagic degradation of ubiquitinated protein aggregates. Its expression is regulated by heat shock factor 1 (HSF1), oxidative stress, and proteasome inhibition. HSPB8 drives autophagy induction and interacts with key pathway components including SQSTM1/p62, LC3, STUB1, and VCP, thereby connecting aggresome processing to protein quality control. Additionally, HSPB8 suppresses caspase activation, linking proteotoxic stress to apoptosis regulation.
In the MH-S alveolar macrophage background, disruption of Hspb8 is predicted to impair chaperone-mediated autophagy, potentially leading to accumulation of misfolded proteins and altered stress resilience. Such proteostasis deficits may influence macrophage phagocytic activity and cytokine secretion, as autophagy intersects with innate immune signaling. This knockout model thus enables dissection of the interplay between protein quality control and pulmonary immune function, and offers a platform to explore macrophage contributions to neurodegenerative pathologies like Charcot-Marie-Tooth disease type 2L and distal hereditary motor neuropathy.
Experimental applications include western blotting and RT-qPCR to verify target disruption and assess downstream effectors, immunofluorescence for aggregate detection, and LC3 turnover assays to measure autophagic flux. Functional readouts such as apoptosis assays, phagocytosis assays, and cytokine profiling permit comprehensive immunophenotyping. The cell line supports drug screening for autophagy modulators and mechanistic investigations into protein aggregation and innate immunity. For additional technical information, please contact Ascent Research.
