Hsp47 (Heat Shock Protein 47), also known as SERPINH1. is a collagen-specific molecular chaperone essential for the proper folding and stabilization of procollagen in the endoplasmic reticulum. It belongs to the serpin family but lacks protease inhibitory activity. Hsp47 binds transiently to nascent procollagen chains, ensuring their triple-helix formation and preventing aggregation or premature degradation. Its expression is stress-inducible and tightly linked to collagen synthesis, making it a critical player in fibrosis, tissue repair, and extracellular matrix (ECM) remodeling.
Hsp47 antibodies are widely used in research to study collagen biosynthesis, fibrotic diseases (e.g., liver cirrhosis, pulmonary fibrosis), and cancer progression, where abnormal ECM deposition occurs. These antibodies enable detection of Hsp47 in various techniques, including Western blotting, immunohistochemistry, and immunofluorescence. Elevated Hsp47 levels are observed in activated fibroblasts (myofibroblasts) and cancer-associated fibroblasts, correlating with disease severity in models of fibrosis or tumor metastasis.
Commercial Hsp47 antibodies are typically raised against specific epitopes of human, mouse, or rat Hsp47. Researchers select antibodies based on host species reactivity, validation in target applications, and compatibility with experimental models. Recent studies also explore Hsp47 inhibition as a therapeutic strategy, emphasizing the antibody's role in validating target engagement in preclinical studies. Proper controls, such as knockout validation, are crucial due to potential cross-reactivity with other serpins or stress-related proteins.