Galectin-3 Protein (GAL3, LGALS3 Protein)

Lectin, Galactoside-binding, soluble, 3

Galectin-3 Products

Galectin-3 Protein, Recombinant

Molecule	Species	Description	Cat. No
Galectin-3/GAL3/LGALS3	Human	Galectin-3 Protein, Recombinant, Native	10289-HNAE
Galectin-3/GAL3/LGALS3	Human	Galectin-3 Protein, Recombinant, Native (Low Endotoxin)	10289-HNAE-E

Galectin-3 cDNA Clone

Molecule	Species	Description	Cat. No
Galectin-3/GAL3/LGALS3	Human	Galectin-3 transcript variant 1 cDNA Clone / ORF Clone	HG10289-M
Galectin-3/GAL3/LGALS3	Mouse	Galectin-3 cDNA Clone / ORF Clone	MG50406-M
Galectin-3/GAL3/LGALS3	Rat	LGALS3 cDNA Clone / ORF Clone	RG80393-G

Galectin-3 Related Areas

Cancer>>Angiogenesis>>Adhesion Molecules in Angiogenesis>>Galectin-3/GAL3/LGALS3

Cancer>>Cancer Biomarkers>>Galectin-3/GAL3/LGALS3

Immunology>>Adhesion Molecule>>Lectin>>Galectin-3/GAL3/LGALS3

Galectin-3 Alternative Names

Galectin-3, LGALS3, GAL3, CBP35, GALBP, GALIG, L31, LGALS2, MAC2 [Homo sapiens]

Galectin-3, Lgals3, gal3, GBP, L-34, Mac-2 [Mus musculus]

Galectin-3 Background

Galectin-3/LGALS3 is a member of the galectin family of carbohydrate binding proteins. Members of this protein family have an affinity for beta-galactosides. This protein is characterized by an N-terminal proline-rich tandem repeat domain and a single C-terminal carbohydrate recognition domain. Galectin-3/LGALS3 can self-associate through the N-terminal domain allowing it to bind to multivalent saccharide ligands. Galectin-3 is promiscuous, its localization within the tissue micro-environment may be extracellular, cytoplasmic, or nuclear, and it has a concentration-dependent ability to be monomeric or form oligomers. Through specific interactions with a variety of intra- and extracellular proteins galectin-3 affects numerous biological processes and seems to be involved in different physiological and pathophysiological conditions, such as development, immune reactions, and neoplastic transformation and metastasis. Galectin-3/LGALS3 plays a role in numerous cellular functions including apoptosis, innate immunity, cell adhesion and T-cell regulation. An early increase in galectin-3 expression identifies failure-prone hypertrophied hearts. Galectin-3/LGALS3 may induce cardiac fibroblast proliferation, collagen deposition, and ventricular dysfunction.

Galectin-3 Related Studies

1. Dumic J, et al. (2006) Galectin-3: an open-ended story. Biochim Biophys Acta. 1760(4): 616-35.
2. Sharma UC, et al. (2004) Galectin-3 marks activated macrophages in failure-prone hypertrophied hearts and contributes to cardiac dysfunction. Circulation. 110(19): 3121-8.
3. Yan YP, et al. (2009) Galectin-3 mediates post-ischemic tissue remodeling. Brain Res. 1288: 116-24.