Human/Mouse/Rat Galectin-3 Antibody Summary
Ala2-Ile264
Accession # P16110
Applications
Mouse Galectin-3 Sandwich Immunoassay
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Detection of Mouse Galectin‑3 by Western Blot. Western blot shows lysates of 4T1 mouse breast cancer cell line, Balb/3T3 mouse embryonic fibroblast cell line and HT-2 mouse T cell line. PVDF membrane was probed with 0.25 µg/mL of Rat Anti-Mouse Galectin-3 Monoclonal Antibody (Catalog # MAB1197) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). A specific band was detected for Galectin-3 at approximately 28 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
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Detection of Human and Rat Galectin‑3 by Western Blot. Western blot shows lysates of MCF-7 human breast cancer cell line, U-118-MG human glioblastoma/astrocytoma cell line, C6 rat glioma cell line, and NR8383 rat alveolar macrophage cell line. PVDF membrane was probed with 0.5 µg/mL of Rat Anti-Mouse Galectin-3 Monoclonal Antibody (Catalog # MAB1197) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). A specific band was detected for Galectin-3 at approximately 28 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
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Detection of Mouse Galectin‑3 by Simple WesternTM. Simple Western lane view shows lysates of HT-2 mouse T cell line and Balb/3T3 mouse embryonic fibroblast cell line, loaded at 0.2 mg/mL. A specific band was detected for Galectin-3 at approximately 43 kDa (as indicated) using 10 µg/mL of Rat Anti-Mouse Galectin-3 Monoclonal Antibody (Catalog # MAB1197) followed by 1:50 dilution of HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
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Detection of Galectin-3 by Western Blot A beta oligomerization and Gal-3 expression are age-dependently increased in APP/PS1 mice. a Wild-type (3 months old) and APP/PS1 mice of different ages (3, 5, 8, and 11 months) were sacrificed and dissected hippocampal tissues were subjected to Western blot analysis for endogenous A beta oligomers. b Quantified results for HMW and LMW A beta oligomerization [n = 4 per group; F(4,15) = 39.3, P < 0.001 for HMW and F(4,15) = 74.07, P < 0.001 for LMW]. Statistical significances for various comparisons are shown in the figure. c Western blot analysis showing the expression levels of Gal-3 and PIAS1 in hippocampal samples from the same batch of WT mice and APP/PS1 mice of different ages (n = 4 per group). d Quantified results for Gal-3 expression in WT and APP/PS1 mice [F(4,15) = 14.59, P < 0.001]. e Quantified results for PIAS1 expression in WT and APP/PS1 mice [F(4,15) = 5.86, P < 0.01] The letter “m” indicates month. Statistical significances of various comparisons are shown in the figure. Data are expressed as mean ± SEM. *P < 0.05, **P < 0.01, #P < 0.001 Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31127200), licensed under a CC-BY license. Not internally tested by R&D Systems.
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Detection of Galectin-3 by Western Blot A beta oligomerization and Gal-3 expression are increased in AD patients. The frontal lobe lysates of normal subjects and AD patients were subjected to Western blot analysis for A beta oligomerization and the expression of Gal-3 and Gal-1 (n = 4 per group). b–d Quantified results for (b) HMW [t(1,6) = 9.72, P < 0.001] and LMW [t(1,6) = 7.21, P < 0.001] A beta oligomerization, c Gal-3 expression [t(1,6) = 4.92, P < 0.01] and d Gal-1 expression [t(1,6) = 0.43, P > 0.05]. e Immunohistochemical analysis showing the distributions of Gal-3 and ProteoStat staining in normal subjects and AD patients (n = 3 per group). Scale bar, 25 μm. DAPI was used to stain nuclei. Data are expressed as mean ± SEM. **P < 0.01, #P < 0.001 Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31127200), licensed under a CC-BY license. Not internally tested by R&D Systems.
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Detection of Galectin-3 by Western Blot Endogenous Gal-3 expression is decreased but memory performance is improved in APP/PS1;Gal-3+/− mice. a Endogenous expression levels of Gal-3 and NEP were examined by Western blot analysis in 3-month-old WT;WT, APP/PS1;WT, WT;Gal-3−/− and APP/PS1;Gal-3+/− mice. b Quantified results for Gal-3 and NEP expression [n = 4 per group; for Gal-3, F(3,12) = 53.47, P < 0.001; q = 10.43, P < 0.001 for the WT;WT group versus the APP/PS1;WT group; q = 6.46, P < 0.001 for the APP/PS1;WT group versus the APP/PS1;Gal-3+/− group and q = 3.98, P < 0.05 for the WT;WT group versus the APP/PS1;Gal-3+/− group; for NEP, F(3,12) = 27.76, P < 0.001; q = 12.04, P < 0.001 for the WT;WT group versus the APP/PS1;WT group; q = 9.72, P < 0.001 for the WT;WT group versus the WT;Gal-3−/− group and q = 6.29, P < 0.01 for the WT;WT group versus the APP/PS1;Gal-3+/− group]. c Acquisition performance obtained by assessing the water maze learning of 8-month-old mice of the four genotypes [n = 7 per group; F(3,24) = 28.72, P < 0.001; q = 9.33, P < 0.001 for the APP/PS1;WT group versus the WT;WT group and q = 3.59, P < 0.05 for the APP/PS1;Gal-3+/− group versus the APP/PS1;WT group]. d Retention performance of the same mice described in (c) [n = 7 per group; F(3,24) = 4.76, P < 0.01; q = 3.94, P < 0.05 for the APP/PS1;WT group versus the WT;WT group; q = 3.25, P < 0.05 for the APP/PS1;Gal-3+/− group versus the APP/PS1;WT group for the target quadrant]. Representative swim patterns from each group are also shown (upper panel). Data are expressed as mean ± SEM. *P < 0.05, **P < 0.01, #P < 0.001 Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31127200), licensed under a CC-BY license. Not internally tested by R&D Systems.
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Detection of Galectin-3 by Western Blot Galectin-3 associates with A beta and interacts with A beta. a Immunohistochemical analysis showing the distributions of endogenous Gal-3 and A beta in hippocampal samples of WT (left panel) and APP/PS1 (right panel) mice at 11 months of age. Scale bar, 200 μm. b Co-IP experiment showing preferential association of Gal-3 with endogenous A beta monomers in 8-month-old APP/PS1 mice. Experiments were performed in duplicate. c Different amounts of recombinant human Gal-3 protein (0.25, 0.5, 1, and 2 μg) were added to a solution containing A beta 42 peptide (15 μg), the mixture was subjected to a thioflavin-T assay, and fluorescence was measured hourly at different time points. The fluorescence plateaued at the 7-h time point. Experiments were performed in triplicate. The abbreviation “rh” indicates “recombinant human”. Data are expressed as mean ± SEM Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31127200), licensed under a CC-BY license. Not internally tested by R&D Systems.
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Detection of Galectin-3 by Immunohistochemistry Tumor derived galectin-3 is a ligand for TREM2. (C) Immunohistochemical staining of galectin-3 in adjacent normal lung & intratumor areas of lung tissues (n = 5). Scale bars, 20 μm. Image collected & cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/39135069), licensed under a CC-BY license. Not internally tested by R&D Systems.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Galectin-3
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 proinflammatory 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).
- Rabinovich, A. et al. (2002) Trends in Immunol. 23:313.
- Rabinovich, A. et al. (2002) J. Leukocyte Biology 71:741.
- Hughes, R.C. (2001) Biochimie 83:667.
- R&D Systems Cytokine Bulletin; Summer 2002.
- Gorski, J.P. et al. (2002) J. Biol. Chem. 277:18840.
Product Datasheets
Citations for Human/Mouse/Rat Galectin-3 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
6
Citations: Showing 1 - 6
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Galectin-3 Negatively Regulates Hippocampus-Dependent Memory Formation through Inhibition of Integrin Signaling and Galectin-3 Phosphorylation
Authors: Yan-Chu Chen, Yun-Li Ma, Cheng-Hsiung Lin, Sin-Jhong Cheng, Wei-Lun Hsu, Eminy H.-Y. Lee
Frontiers in Molecular Neuroscience
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Postpartum administration of eplerenone to mitigate vascular dysfunction in mice following a preeclampsia-like pregnancy
Authors: Binder, NK;de Alwis, N;Beard, S;Fato, BR;Garg, A;Baird, L;Young, MJ;Hannan, NJ;
Scientific reports
Species: Mouse
Sample Types: Whole Tissue
Applications: Immunohistochemistry -
Galectin-3 promotes A&beta oligomerization and A&beta toxicity in a mouse model of Alzheimer's disease
Authors: CC Tao, KM Cheng, YL Ma, WL Hsu, YC Chen, JL Fuh, WJ Lee, CC Chao, EHY Lee
Cell Death Differ., 2019-05-24;27(1):192-209.
Species: Rat
Sample Types: Hippocampal Cell Lysates
Applications: Western Blot -
Proteomic and functional analysis identifies galectin-1 as a novel regulatory component of the cytotoxic granule machinery
Authors: T Clemente, NJ Vieira, JP Cerliani, C Adrain, A Luthi, MR Dominguez, M Yon, FC Barrence, TB Riul, RD Cummings, TM Zorn, S Amigorena, M Dias-Baruf, MM Rodrigues, SJ Martin, GA Rabinovich, GP Amarante-M
Cell Death Dis, 2017-12-07;8(12):e3176.
Species: Human
Sample Types: Cell Lysates
Applications: Western Blot -
Galectin-3 negatively regulates the frequency and function of CD4(+) CD25(+) Foxp3(+) regulatory T cells and influences the course of Leishmania major infection.
Authors: Fermino M, Dias F, Lopes C, Souza M, Cruz A, Liu F, Chammas R, Roque-Barreira M, Rabinovich G, Bernardes E
Eur J Immunol, 2013-05-17;43(7):1806-17.
Species: Mouse
Sample Types: Whole Tissue
Applications: IHC-Fr -
The receptor of advanced glycation end products plays a central role in advanced oxidation protein products-induced podocyte apoptosis.
Kidney Int, 2012-05-23;82(7):759-70.
Species: Mouse
Sample Types: Whole Cells
Applications: Neutralization
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