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 # ...read more
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Galectin-3 Antibody [Allophycocyanin] Summary
Immunogen
E. coli-derived recombinant human Galectin-3 Ala2-Ile250 Accession # P17931.5
Specificity
Detects human Galectin-3 in direct ELISAs and Western blots. In direct ELISAs and Western blots, approximately 50% cross-reactivity with recombinant mouse Galectin-3 is observed and less than 1% cross-reactivity with recombinant human Galectin-1, -2, -4, -7, and -8 is observed.
Source
N/A
Isotype
IgG
Clonality
Polyclonal
Host
Goat
Gene
LGALS3
Purity
Antigen Affinity-purified
Purity Statement
Antigen Affinity-purified
Innovator's Reward
Test in a species/application not listed above to receive a full credit towards a future purchase.
Alternate Names for Galectin-3 Antibody [Allophycocyanin]
AGE-R3
Carbohydrate-binding protein 35
CBP 35,35 kDa lectin
CBP35
GAL3
Gal-3
galactin-3
Galactose-specific lectin 3
Galactoside-binding protein
GALBPCBP35
Galectin3
Galectin-3
GALIG
IgE-binding protein
L29
L31
L-31
Laminin-binding protein
Lectin L-29
lectin, galactoside-binding, soluble, 3
LGALS2
LGALS3
Mac-2 antigen
Mac-2
MAC2GAL3
Background
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).
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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