HSPB11 (Heat Shock Protein Family B [Small] Member 11), also known as HSPCO029 or DKFZp686O24198. is a member of the small heat shock protein (sHSP) family. These proteins are characterized by their conserved α-crystallin domain and function as molecular chaperones, aiding in protein folding, preventing aggregation under stress, and maintaining cellular homeostasis. HSPB11 is distinct from classical sHSPs like HSPB1 (HSP27) due to its unique structural features and expression patterns. It is ubiquitously expressed, with higher levels observed in tissues such as the liver, kidney, and testis.
Research suggests HSPB11 participates in diverse cellular processes, including endoplasmic reticulum (ER) stress response, apoptosis regulation, and cell proliferation. It interacts with key ER stress sensors like PERK and IRE1α, implicating its role in the unfolded protein response (UPR). Dysregulation of HSPB11 has been linked to pathological conditions, such as cancer (e.g., hepatocellular carcinoma, colorectal cancer) and neurodegenerative disorders, where its overexpression or suppression correlates with disease progression.
HSPB11 antibodies are critical tools for studying its expression, localization, and function. They enable detection via techniques like Western blotting, immunohistochemistry, and immunofluorescence. Commercially available antibodies are typically validated for specificity using knockout cell lines or siRNA-mediated knockdown. These reagents support investigations into HSPB11's mechanistic roles in stress adaptation, disease pathways, and potential therapeutic targeting. However, variability in antibody performance across applications necessitates careful validation for experimental reproducibility.