Immobilized Recombinant Mouse Galectin-9 (Catalog # 3535-GA)supports the adhesion of D10.G4.1 mouse helper T cells. The ED50 forthis effect is 0.6-3 μg/mL.
>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
36.4 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.
SDS-PAGE
36 kDa, reducing conditions
Publications
Read Publications using 3535-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.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in MOPS, NaCl, EDTA, DTT 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 sterile, deionized water.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Galectin-9 Protein, CF
Ecalectin
GAL9
gal-9
galectin 9
Galectin9
Galectin-9
HUAT
lectin, galactoside-binding, soluble, 9
LGALS9
LGALS9A
MGC117375
MGC125973
MGC125974
Tumor antigen HOM-HD-21
urate transporter/channel protein
Background
Galectins comprise a family of multifunctional carbohydrate-binding proteins with specificity for N-acetyl-lactosamine-containing glycoproteins. At least 14 mammalian Galectins share structural similarities in their carbohydrate recognition domains (CRD), forming three groups: a prototype group (one CRD), a tandem‑repeat group (two CRDs), and a chimeric group (one CRD, unique N-terminus) (1, 2). Full length Galectin-9 is a widely expressed 39 kDa tandem‑repeat group Galectin that contains two CRDs connected by a linker region (3). Alternate splicing generates an extended, small intestine-specific isoform with a 31 amino acid insertion in the linker region (3). The standard (or short) isoform of mouse Galectin-9 is orthologous to human galectin-9, which is also known as Ecalectin (4). This isoform shares 70% and 85% aa sequence identity with the corresponding regions of human and rat Galectin-9, respectively. Galectin-9 exhibits a wide range of activities including eosinophil chemoattraction (5-7). This activity is destroyed by thrombin-mediated cleavage within the linker region of the long isoform, although the human Ecalectin isoform is resistant to thrombin (8). Galectin-9 binds to carbohydrate moieties of IgE, thereby preventing immune complex formation, mast cell degranulation, and asthmatic and cutaneous anaphylaxis reactions (9). Independent of its lectin properties, Galectin-9 induces the maturation of dendritic cells which promote Th1 polarization (10). Galectin-9 induces cellular apoptosis in part by direct binding to TIM-3 (11, 12). Its interaction with TIM-3 inhibits Th1 cell and CD8+ cytotoxic T cell responses, while also promoting regulatory T cell differentiation and activity (12, 13). Conversely, Galectin-9 is also reported to bind to a non-TIM3 receptor on both Th1 and Th2 cells, promoting both apoptosis and cytokine secretion, suggesting multiple receptors on T helper cells (14). Galectin-9 suppresses tumor cell metastasis by interfering with the associations between hyaluronic acid and CD44 and between VCAM-1 and Integrin alpha 4 beta 1 (15). Galectin-9, also known as the UAT or urate transporter, can also be expressed as an integral membrane protein in kidney that mediates the cellular efflux of urate (16).
Zhu, C. et al. (2011) Curr. Top. Microbiol. Immunol. 350:1.
Elola, M.T. et al. (2007) Cell. Mol. Life Sci. 64:1679.
Wada, J. and Y.S. Kanwar (1997) J. Biol. Chem. 272:6078.
Matsushita, N. et al. (2000) J. Biol. Chem. 275:8355.
Matsumoto, R. et al. (2002) J. Immunol. 168:1961.
Chabot, S. et al. (2002) Glycobiology 12:111.
Sato, M. et al. (2002) Glycobiology 12:191.
Nishi, N. et al. (2006) Glycobiology 16:15C.
Niki, T. et al. (2009) J. Biol. Chem. 284:32344.
Dai, S.-Y. et al. (2005) J. Immunol. 175:2974.
Seki, M. et al. (2007) Arthritis Rheum. 56:3968.
Zhu, C. et al. (2005) Nat. Immunol. 6:1245.
Sehrawat, S. et al. (2010) PloS Pathogens 6:e1000882.
Su, E.W. et al. (2011) Glycobiology 21:1258.
Nobumoto, A. et al. (2008) Glycobiology 18:735.
Leal-Pinto, E. et al. (2002) Am. J. Physiol. Renal Physiol. 283:F150.
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