Recombinant Human Galectin-1 Protein Summary
Product Specifications
Ala2-Asp135
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
1152-GA
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS and Betamercaptoethanol with BSA as a carrier protein. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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1152-GA/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS and Betamercaptoethanol. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Scientific Data
2 μg/lane of Recombinant Human Galectin-1 Protein (Catalog # 1152-GA) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 11-14 kDa.
Reconstitution Calculator
Background: Galectin-1
Galectin-1, gene name LGALS1 (lectin, galactoside-binding, soluble 1), is a 135 amino acid (aa), 14 kDa, pleiotropic, non-glycosylated, monomeric or homodimeric carbohydrate-binding protein of the prototype galectin family (1-3). Galectins lack a classical signal peptide and can be localized to the cytosolic compartments, or secreted via non-classical pathways (1). Secreted Galectin-1 has immunosuppressive and anti-inflammatory properties and suppresses acute and chronic inflammation and autoimmunity. It contributes to negative selection of developing T cells, immunosuppression by regulatory T cells, resolution of the inflammatory response, and inhibition of immune cell migration, inflammatory cytokine production, and mast cell degranulation (1, 2, 4-6). Galectin-1 preferentially binds laminin, fibronectin, 90K/Mac-2BP, CD45, CD43, CD7, CD2, CD3, integrins alpha 4 beta 1, alpha 5 beta 1 and alpha 4 beta 7, and ganglioside GM1 (2, 3). It is produced in a variety of tissues by cells that include endothelial cells, connective tissue fibroblasts, thymic stromal cells, tumor cells, muscle cells, platelets, regulatory T cells, and activated tissue macrophages, B cells, T cells and dendritic cells (2, 3, 6-11). Most of this expression is cytosolic. Human Galectin-1 shares 88% aa sequence identity with mouse, equine and ovine, 90% with rat, and 87% with bovine and porcine Galectin-1. Endothelial cell surface expression, including tumor endothelial cells, is greatly increased by cell activation (9). Galectin-1 is highly expressed at the maternal-fetal interface and contributes to fetal immune privilege (5, 12). Its immunosuppressive properties appear to also allow tumor cells to evade immune detection (4, 5). It selectively controls T cell survival by inducing apoptosis of activated Th1 and Th17 cells, which express Galectin-1-binding glycans, while promoting Th2 cell survival where glycans are sialylated and less recognized (4, 13). It also induces apoptosis of immature thymocytes (3, 6). Galectin-1 secreted from bone marrow stromal cells aids B lymphocyte development by contributing to pre-B cell integrin adhesion and receptor signaling (3). The dimer form of Galectin-1 also induces neutrophil down‑regulation by inducing cell surface exposure of phosphatidylserine that marks the cell for phagocytosis (14). Galectin-1 can also modulate cell-cell and cell-matrix interactions, and can promote either cell attachment or detachment depending on the cell type and developmental stage (1, 2).
- Di Lella, S. et al. (2011) Biochemistry 50:7842.
- Rabinovich, G.A. and J.M. Ilarregui (2009) Immunol. Rev. 230:144.
- Rabinovich, G.A. and M. Vidal. (2011) Curr. Opin. Hematol. 18:443.
- Cedeno-Laurent, F. and C.J. Dimitroff (2012) Clin. Immunol. 142:107.
- Than, N.G. et al. (2012) Trends Endocrinol. Metab. 23:23.
- Rubinstein, N. et al. (2004) Tissue Antigens 64:1.
- Courad, P.O. et al. (1989) J. Biol. Chem. 264:1310.
- Hirabayashi, J. et al. (1989) Biochim. Biophys. Acta 1008:85.
- Thijssen, V.L. et al. (2008) Am. J. Pathol. 172:545.
- Nio-Kobayashi, J. et al. (2009) J. Histochem. Cytochem. 57:41.
- Dias-Baruffi, M. et al. (2010) Glycobiology 20:507.
- Than, N.G. et al. (2008) Proc. Natl. Acad. Sci. USA 105:15819.
- Toscano, M.A. et al. (2007) Nat. Immunol. 8:825.
- Stowell, S.R. et al. (2009) J. Biol. Chem. 284:4989.
Citations for Recombinant Human Galectin-1 Protein
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.
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Citations: Showing 1 - 6
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Serum galectin-1 in patients with multiple myeloma: associations with survival, angiogenesis, and biomarkers of macrophage activation
Authors: MN Andersen, M Ludvigsen, N Abildgaard, I Petruskevi, R Hjortebjer, M Bjerre, B Honoré, HJ Møller, NF Andersen
Onco Targets Ther, 2017-04-04;10(0):1977-1982.
Species: Human
Sample Types: Serum
Applications: ELISA Standard -
Galectin-1-Induced Autophagy Facilitates Cisplatin Resistance of Hepatocellular Carcinoma.
Authors: Su Y, Davuluri G, Chen C, Shiau D, Chen C, Chen C, Lin Y, Chang C
PLoS ONE, 2016-02-09;11(2):e0148408.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Induction of galectin-1 by TGF-beta1 accelerates fibrosis through enhancing nuclear retention of Smad2.
Authors: Lim M, Ahn J, Yi J, Kim M, Son A, Lee S, Lim D, Kim S, Kang M, Han Y, Song J
Exp Cell Res, 2014-06-11;326(1):125-35.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Morphine and galectin-1 modulate HIV-1 infection of human monocytes-derived macrophages
Authors: Jessica L. Reynolds, Wing Cheung Law, Supriya D. Mahajan, Ravikumar Aalinkeel, Bindukumar Nair, Donald E. Sykes et al.
The Journal of Immunology
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Binding of Toxoplasma gondii glycosylphosphatidylinositols to galectin-3 is required for their recognition by macrophages.
Authors: Debierre-Grockiego F, Niehus S, Coddeville B, Elass E, Poirier F, Weingart R, Schmidt RR, Mazurier J, Guerardel Y, Schwarz RT
J. Biol. Chem., 2010-08-20;285(43):32744-50.
Species: Bacteria
Sample Types: Complex Sample Type
Applications: Surface Plasmon Resonance -
Equine umbilical cord blood contains a population of stem cells that express Oct4 and differentiate into mesodermal and endodermal cell types.
Authors: Reed SA, Johnson SE
J. Cell. Physiol., 2008-05-01;215(2):329-36.
Species: Equine
Sample Types: Whole Cells
Applications: Bioassay
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Average Rating: 5 (Based on 2 Reviews)
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Reason for Rating: Works well from growing cells.