Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to support the adhesion of MOLT‑4 human acute lymphoblastic leukemia cells. The ED50 for this effect id 0.6-3 μg/mL. 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 3-10 μg/mL. |
Source | Human embryonic kidney cell, HEK293-derived human Galectin-3 protein Ala2-Ile250 |
Accession # | |
N-terminal Sequence | No results obtained: Ala2 predicted. |
Protein/Peptide Type | Recombinant Proteins |
Gene | LGALS3 |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 25 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. |
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SDS-PAGE | 26-31 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in HEPES, NaCl, TCEP, PEG and Trehalose. |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in PBS. |
Human 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 human Galectin-3 shares 78% and 79% amino acid (aa) sequence identity with mouse and rat Galectin-3, respectively. Human 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 crosslinking 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).
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