Biglycan is a small leucine-rich proteoglycan (SLRP) predominantly found in the extracellular matrix (ECM) of connective tissues, including bone, cartilage, and blood vessels. It plays critical roles in ECM assembly, collagen fibrillogenesis, and cellular signaling by interacting with growth factors (e.g., TGF-β) and cell surface receptors. Dysregulation of biglycan is linked to pathologies such as osteoporosis, cardiovascular diseases, fibrosis, and cancer, where it modulates inflammation, angiogenesis, and tumor progression.
Antibodies targeting biglycan are essential tools for studying its expression, localization, and function. These antibodies, often produced in rabbits or mice, enable detection via techniques like Western blotting, immunohistochemistry, and immunofluorescence. Specificity is validated using knockout models or siRNA-mediated silencing. Monoclonal antibodies (e.g., clone 7F1) offer high reproducibility, while polyclonal variants may detect multiple epitopes.
Research applications include investigating biglycan's role in ECM remodeling, its crosstalk with Toll-like receptors (TLRs) in innate immunity, and its dual pro- or anti-tumor effects depending on context. Commercial antibodies are widely used in biomarker studies, particularly in osteoarticular and cardiovascular research, aiding therapeutic target discovery. Proper validation remains crucial to avoid cross-reactivity with related SLRPs like decorin.