BLVRB (biliverdin reductase B) is a key enzyme in the heme catabolism pathway, responsible for reducing biliverdin IXβ to bilirubin IXβ using NADPH as a cofactor. This reaction is critical for maintaining cellular redox balance, as bilirubin acts as an endogenous antioxidant. BLVRB is distinct from its isoform BLVRA (biliverdin reductase A), which primarily reduces biliverdin IXα. While BLVRA is ubiquitously expressed, BLVRB shows tissue-specific expression, particularly in the liver, spleen, and macrophages, where heme degradation is most active.
Antibodies targeting BLVRB are essential tools for studying its biological roles, including its involvement in iron recycling, inflammation modulation, and cellular stress responses. Researchers use BLVRB antibodies in techniques like Western blotting, immunohistochemistry, and ELISA to quantify protein levels, assess localization, and explore regulatory mechanisms. BLVRB's association with disorders like Gilbert's syndrome, anemia, and neurodegenerative diseases has driven interest in its functional characterization. Structural studies reveal BLVRB belongs to the short-chain dehydrogenase/reductase family, featuring a Rossmann-fold NADPH-binding domain. However, its enzymatic activity and non-enzymatic signaling roles (e.g., kinase regulation) remain under investigation. Commercial BLVRB antibodies are typically validated for specificity against unique epitopes, given the high sequence similarity (~35%) between BLVRB and BLVRA. Recent studies also implicate BLVRB in cancer progression and drug resistance, expanding its potential therapeutic relevance.