Lumican, a member of the small leucine-rich proteoglycan (SLRP) family, plays a critical role in regulating collagen fibril organization and extracellular matrix (ECM) stability. It is expressed in various tissues, including the cornea, skin, and cartilage, and is involved in cell migration, tissue repair, and immune response modulation. Lumican’s core protein (～38-42 kDa) contains leucine-rich repeats that mediate collagen binding, while its glycosaminoglycan (GAG) chains influence hydration and ECM interactions.
Lumican antibodies are essential tools for studying its biological functions and pathological roles. In research, these antibodies are used in techniques like immunohistochemistry, Western blotting, and ELISA to detect Lumican expression, localization, and post-translational modifications. They have revealed Lumican’s dual role in cancer—acting as a tumor suppressor by inhibiting metastasis in some contexts (e.g., breast cancer) or promoting progression in others (e.g., pancreatic cancer).
Clinically, Lumican antibodies aid in diagnosing corneal diseases, as Lumican mutations are linked to corneal opacity disorders. They also explore Lumican’s potential as a biomarker in fibrosis, osteoarthritis, and wound healing. Commercially available antibodies are often raised against specific epitopes (human, mouse, or recombinant proteins) and validated for cross-reactivity. Challenges include distinguishing Lumican isoforms and ensuring specificity due to structural similarities within the SLRP family. Ongoing studies focus on therapeutic targeting of Lumican pathways in ECM-related pathologies.