Anti-Human/Mouse Mac-2 (Galectin-3) (Clone M3/38 ) - PE (M362-GRP)

Mac-2 (Galectin-3) is a β-galactoside-binding lectin of the chimera-type, characterized by a single carbohydrate recognition domain and an N-terminal polypeptide tail region1. Mac-2 plays important roles in cell proliferation, apoptotic regulation, cell-to-cell and cell-to-matrix interactions, macrophage activation, angiogenesis, inflammation, fibrosis and host defense. Additionally, Mac-2 is an early-stage diagnostic and/or prognostic biomarker for viral infection, neurodegenerative disorders, tumor formation, diabetes mellitus, and certain types of heart, kidney, and autoimmune disease. The primary structure of mouse and human Mac-2 is highly conserved with 85% similarity2. Human Mac-2 binds to asialofetuin and purified laminin. M3/38 was generated by immunizing rats with immunoadsorbent-purified macrophage glycoproteins and fusing the resulting spleen cells with mouse myeloma cells3. M3/38 is able to immunoprecipitate both the mouse and human Mac-2 homologs2,3. M3/38 binding to Mac-2 can be inhibited by galactose2. M3/38 recognizes a linear epitope within the N-terminal domain of Mac-24. The common minimal sequence as determined by SPOT analysis as Ala-Pro-Pro-Gly-Ala-Tyr. M3/38 has been exploited for live cell thyroid tumor imaging4,5. A chimeric M3/38 Fab-fragment and its humanized derivative can detect Mac-2 overexpression in cancerous thyroid nodules in mice via positron emission tomography. The three-dimensional structure of the rat/human chimeric Fab has been determined5.