|Detection of Human, Mouse, and Rat HSPB8 by Western Blot. Western blot shows lysates of human, mouse, and rat heart tissue. PVDF Membrane was probed with 0.5 µg/mL of Mouse Anti-Human/Mouse/Rat HSPB8 Monoclonal Antibody (Catalog # MAB4987) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for HSPB8 at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.|
Heat shock protein beta-8 (HSPB8, also HSP22 or CRYAC) is a 22‑25 kDa member of the small HSP (HSP20) family of proteins. It is expressed in muscle (smooth, skeletal and cardiac), and serves as a molecular chaperone. Human HSPB8 contains one alpha -crystalline domain (aa 93‑170) that mediates protein-protein interaction, and N- plus C-terminal flanking sequences that generate homodimers, homooligomers, and heterodimers with HSP27 and HSPB7. Phosphorylation at Ser57 blocks HSPB8 chaperone activity. Human HSPB8 shares 94% aa identity with both mouse and canine HSPB8. Deficiencies in HSPB8 are involved in distal motor neuropathy type 11A.
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