Measured by its ability to agglutinate human red blood cells. Hadari, Y.R. et al. (2000) J. Cell Sci. 113:2385. The ED50 for this effect is 5‑20 µg/mL.
Source
E. coli-derived mouse Galectin-3 protein Ala2-Ile264
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
27.3 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using 1197-GA in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
3 months, 2 to 8 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS, EDTA and DTT with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 250 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Galectin-3 Protein
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
Galectin-3, also known as Mac-2, L29, CBP35, and epsilon BP, is classified as a chimeric member of the Galectin superfamily and contains one carbohydrate recognition domain (CRD) linked to a nonlectin domain (1, 2). Mature mouse Galectin-3 shares 80% and 86% amino acid (aa) sequence identity with human and rat Galectin-3, respectively. Galectin-3 is a 26 kDa protein that can be nuclear, cytoplasmic, or secreted (3, 4). Nuclear Galectin-3 can modulate gene expression, while cytosolic Galectin-3 can inhibit apoptosis and can participate in exocytosis, Caveolin-mediated endocytosis, and macrophage-mediated clearance of apoptotic cells (5-7). Extracellular Galectin-3 has been shown to form high-order oligomers that promote the cross-linking of cell surface oligosacchraides as well as integrin-dependent cell adhesion and apoptosis (8-11). Galectin-3 contributes to the innate immune response against Candida albicans and Streptococcus pneumoniae, and it can facilitate acute inflammatory responses via neutrophil activation and opsonization, macrophage recruitment, and mast cell activation (12-14). Galectin-3 can also contribute to chronic inflammation and fibrosis (15). It is implicated in neuroinflammatory disorders of the central nervous system, cardiac fibrosis, and heart failure, as well as tumor growth, progression, and metastasis (16-18).
Robertson, M.W. et al. (1990) Biochemistry 29:8093.
Elola, M.T. et al. (2007) Cell. Mol. Life Sci. 64:1679.
Haudek, K.C. et al. (2010) Biochim. Biophys. Acta 1800:181.
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