HSPB8. also known as heat shock protein beta-8 or HSP22. is a member of the small heat shock protein (sHSP) family. These proteins function as molecular chaperones, aiding in the refolding of misfolded proteins and preventing aggregation under stress conditions. HSPB8 is particularly notable for its role in cellular quality control mechanisms, including chaperone-assisted selective autophagy (CASA), which targets damaged proteins and organelles for degradation. It is expressed in various tissues, with high levels observed in skeletal muscle, the nervous system, and the heart. Dysregulation of HSPB8 has been linked to neurodegenerative diseases (e.g., Alzheimer's, ALS) and myopathies, as mutations or altered expression can disrupt protein homeostasis, leading to toxic aggregate accumulation.
Antibodies against HSPB8 are essential tools for studying its expression, localization, and function in both physiological and pathological contexts. They are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to detect HSPB8 in tissue samples or cell cultures. Researchers also employ these antibodies to investigate HSPB8's interaction with other proteins, such as BAG3. in autophagy pathways or its role in stress response signaling. Commercially available HSPB8 antibodies are typically raised in rabbits or mice, with validation across multiple applications. Specificity and cross-reactivity remain critical considerations, given the structural similarities among sHSP family members. Studies utilizing HSPB8 antibodies have advanced therapeutic strategies targeting protein aggregation diseases, emphasizing its potential as a biomarker or intervention target.