HSPB1 (Heat Shock Protein Family B Member 1) is a small molecular chaperone that maintains protein homeostasis and regulates multiple cellular processes. As a molecular chaperone, HSPB1 prevents protein aggregation and maintains denatured proteins in a folding-competent state 1. The protein plays crucial roles in stress resistance and cellular protection by inhibiting apoptosis and ferroptosis through antioxidant mechanisms 23. HSPB1 directly interacts with key proteins including TDP-43, regulating cytoplasmic phase separation and preventing pathological aggregation associated with neurodegeneration 1. In neurodegenerative diseases, reactive astrocytes secrete HSPB1 to provide non-cell-autonomous neuroprotection, reducing inflammatory responses and tau inclusions 4. The protein also restores autophagic flux by facilitating dissociation of autophagy receptors from poly-glycine aggregates 5. Clinically, HSPB1 mutations cause Charcot-Marie-Tooth disease through altered oligomerization and reduced chaperone activity 6. In cancer, HSPB1 promotes chemoresistance by protecting cells from drug-induced ferroptosis via NF-κB signaling activation 7. HSPB1 expression correlates with tumor progression and poor prognosis, making it both a biomarker and potential therapeutic target across multiple diseases 8.