Human Galectin-3 ELISA Kit

Galectin-3, also known as Mac-2, 35 kDa lectin, carbohydrate-binding protein 35 (CBP 35), galactose-specific lectin 3, galactoside-binding protein (GALBP), IgE-binding protein, is a member of the carbohydrate-binding protein family in which at least 14 mammalian galectins have been identified so far. Structurally, Galectins are characterized by the carbohydrate-recognition-binding domain (CRD) that is required for the specific binding of beta-galactosides. Galectin-3 is expressed in the nucleus, cytoplasm, mitochondrion, cell surface, and extracellular space. Human Galectin-3 is widely expressed in various cells, including macrophages, activated T cells, osteoclasts, epithelial cells, tumor cells, and fibroblasts. Human Galectin-3 shares approximately 86% amino acid (aa) sequence identity with mouse counterpart. Galectin-3 interacts with numerous partners extracellularly and intracellularly. For example, The Galectin-3 CRD recognizes terminal, unsialated LacNAc structures that are present on approximately 20% of all serum proteins and many extracellular matrix proteins, while its eight tandem repeats within the unique N-terminal domain participate in protein-protein interactions. Extracellular Galectin-3 is involved in innate immunity, binding carbohydrates on specific pathogens and acting as an opsonin. It is chemotactic for macrophages and induces innate immune responses in neutrophils. It participates in lipid rafts and influences receptor dimerization or clustering, potentially regulating signaling, adhesion, and receptor endocytosis. In the cytosol, it can inhibit apoptosis and participate in exocytosis, caveolin-mediated endocytosis, and macrophage clearance of apoptotic cells, while nuclear Galectin-3 plays a role in regulating gene expression. Clinically, increased serum Galectin-3 has been associated with rheumatoid arthritis, Behceta€s disease, and a variety of cancers, especially when they are metastatic.

156-10, 000pg/mL

100 uL final volume, dilution factor varies on samples