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Heat shock protein family A member 1B (HSPA1B), also called HSP70-2 or HSP72, is a molecular chaperone belonging to the HSP70 family[2][3]. It is a 70 kDa protein encoded by an intronless gene located in the MHC class III region of chromosome 6[2]. HSPA1B is rapidly upregulated in response to cellular stress (such as heat shock, oxidative damage, infection), where it stabilizes unfolded or misfolded proteins and prevents aggregation by promoting refolding or targeting proteins for degradation through the ubiquitin-proteasome pathway[2][3]. HSPA1B plays a critical role in maintaining protein homeostasis, regulating apoptosis, and modulating immune responses (including acting as a receptor for viral entry)[2]. Overexpression or dysregulation of HSPA1B is implicated in cancer progression, inflammatory diseases, infections, neurodegenerative diseases, and cardiovascular conditions[2][3]. HSPA1B is a key target for therapeutics aiming to control protein quality, apoptosis, and cellular stress responses.
Inhibition of ATPase activity; Disruption of chaperone-mediated protein folding; Modulation of stress response; Induction of apoptosis via protein misfolding; Promotion of protein degradation
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