Human Galectin-3 APC-conjugated Antibody Summary
Accession # P17931.5
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Galectin‑3 in Human Blood Monocytes by Flow Cytometry. Human peripheral blood monocytes were stained with Goat Anti-Human Galectin-3 APC-conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # IC1154A, filled histogram) or isotype control antibody (Catalog # IC108A, open histogram). To facilitate intracellular staining, cells were fixed with Flow Cytometry Fixation Buffer (Catalog # FC004) and permeabilized with Flow Cytometry Permeabilization/Wash Buffer I (Catalog # FC005). View our protocol for Staining Intracellular Molecules.
Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
The galectins constitute a large family of carbohydrate-binding proteins with specificity for N-acetyl-lactosamine-containing glycoproteins. At least 14 mammalian galectins, which share structural similarities in their carbohydrate recognition domains (CRD), have been identified. The galectins have been classified into the prototype galectins (-1, -2, -5, -7, -10, -11, -13, -14), which contain one CRD and exist either as a monomer or a noncovalent homodimer; the chimera galectins (Galectin-3) containing one CRD linked to a nonlectin domain; and the tandem-repeat galectins (-4, -6, -8, -9, -12) consisting of two CRDs joined by a linker peptide. Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However, via one or more as yet unidentified non-classical secretory pathways, galectins can also be secreted to function extracellularly. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell-surface glycoproteins (1-4).
Galectin-3, also known as Mac-2, L29, CBP35, and epsilon BP, is a chimera galectin that has a tendency to dimerize. Besides the soluble protein, alternatively spliced forms of chicken Galectin-3 containing a transmembrane-spanning domain and a leucine zipper motif have been reported. Galectin-3 is expressed in tumor cells, macrophages, activated T cells, osteoclasts, epithelial cells, and fibroblasts. It binds various matrix glycoproteins including laminin, fibronectin, LAMPS, 90K/Mac-2BP, MP20, and CEA. Galectin-3 promotes cell growth and proliferation for many cell types. Galectin-3 acts intracellularly to prevent apoptosis. Depending on the cell types, Galectin-3 exhibits pro- or anti-adhesive properties. Galectin-3 has pro-inflammatory activities in vitro and in vivo. It induces pro-inflammatory and inhibits Th2 type cytokine production. Galectin-3 chemoattracts monocytes and macrophages. It activates and degranulates basophils and mast cells. Elevated circulating levels of Galectin-3 has been show to correlate with the malignant potential of several types of cancer, suggesting that Galectin-3 is also involved in tumor growth and metastasis. Human and mouse Galectin-3 shares approximately 80% amino acid sequence similarity (1-5).
- Rabinovich, A. et al. (2002) Trends in Immunol. 23:313.
- Rabinovich, A. et al. (2002) J. Leukocyte Biology 71:741.
- Hughes, R.C. (2001) Biochimie 83:667.
- R&D Systems Cytokine Bulletin; Summer 2002.
- Gorski, J.P. et al. (2002) J. Biol. Chem. 277:18840.
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