R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Galectin-3/LGALS3 (E7B6R) Rabbit mAb #89572
Filter:
- WB
- IP
- IHC
- IF
Western blot analysis of extracts from various cell lines using Galectin-3/LGALS3 (E7B6R) Rabbit mAb (upper) and β-Actin (D6A8) Rabbit mAb #8457 (lower).
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 28 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IHC-Immunohistochemistry
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Related Products
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
| Immunohistochemistry (Paraffin) | 1:50 - 1:200 |
| Immunofluorescence (Frozen) | 1:100 - 1:400 |
| Immunofluorescence (Immunocytochemistry) | 1:800 - 1:3200 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
For a carrier free (BSA and azide free) version of this product see product #76015.
For a carrier free (BSA and azide free) version of this product see product #76015.
Protocol
Specificity / Sensitivity
Galectin-3/LGALS3 (E7B6R) Rabbit mAb recognizes endogenous levels of total Galectin-3/LGALS3 protein. This antibody recognizes mouse Galectin-3/LGALS3 protein and is also reactive with human Galectin-3/LGALS3; however, this antibody is not suggested for immunohistochemical analysis of human tissues.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly15 of mouse Galectin-3/LGALS3 protein.
Background
Galectins are a family of β-galactose binding proteins that are characterized by an affinity for poly-N-acetyllactosamine-enriched glycoconjugates and a carbohydrate-binding site (1,2). Members of the galectin family have been implicated in a variety of biological functions, including cell adhesion (3), growth regulation (4), cytokine production (5), T cell apoptosis (6), and immune responses (7).
Galectin-3/LGALS3 is involved in several diverse biological functions. Galectin-3/LGALS3 binds IgE (8). Galectin-3/LGALS3 is an unusual protein in that it can be found both extracellularly and intracellularly. Intracellularly, Galectin-3/LGALS3 can localize to the cytoplasm, nucleus, or both, depending on cell type and experimental conditions. Nuclear Galectin-3/LGALS3 has been identified as a pre-mRNA splicing factor (9). Galectin-3/LGALS3 production has been shown to increase during inflammation and in obesity, and the protein itself can have an inflammatory effect under certain conditions (10). Galectin-3/LGALS3 forms a complex with α3, β1 integrin to act as a surface receptor on endothelial cells for the NG2 proteoglycan, which triggers cell motility and angiogenesis (11). In addition to these functions, Galectin-3/LGALS3 is also a required factor for the terminal differentiation of epithelial cells (12).
Galectin-3/LGALS3 is involved in several diverse biological functions. Galectin-3/LGALS3 binds IgE (8). Galectin-3/LGALS3 is an unusual protein in that it can be found both extracellularly and intracellularly. Intracellularly, Galectin-3/LGALS3 can localize to the cytoplasm, nucleus, or both, depending on cell type and experimental conditions. Nuclear Galectin-3/LGALS3 has been identified as a pre-mRNA splicing factor (9). Galectin-3/LGALS3 production has been shown to increase during inflammation and in obesity, and the protein itself can have an inflammatory effect under certain conditions (10). Galectin-3/LGALS3 forms a complex with α3, β1 integrin to act as a surface receptor on endothelial cells for the NG2 proteoglycan, which triggers cell motility and angiogenesis (11). In addition to these functions, Galectin-3/LGALS3 is also a required factor for the terminal differentiation of epithelial cells (12).
- Barondes, S.H. et al. (1994) Cell 76, 597-8.
- Barondes, S.H. et al. (1994) J Biol Chem 269, 20807-10.
- Offner, H. et al. (1990) J Neuroimmunol 28, 177-84.
- Wells, V. and Mallucci, L. (1991) Cell 64, 91-7.
- Filer, A. et al. (2009) Arthritis Rheum 60, 1604-14.
- Perillo, N.L. et al. (1995) Nature 378, 736-9.
- Cooper, D.N. et al. (1991) J Cell Biol 115, 1437-48.
- Platzer, B. et al. (2011) Immunol Lett 141, 36-44.
- Haudek, K.C. et al. (2010) Biochim Biophys Acta 1800, 181-9.
- Pang, J. et al. (2013) PLoS One 8, e57915.
- Fukushi, J. et al. (2004) Mol Biol Cell 15, 3580-90.
- Hikita, C. et al. (2000) J Cell Biol 151, 1235-46.
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