Recombinant Human Galectin-9 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 9064-GA

R&D Systems, part of Bio-Techne
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9064-GA-050
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Key Product Details

Source

HEK293

Accession #

NP_002299

Conjugate

Unconjugated

Applications

Bioactivity

View all Galectin-9 Proteins and Enzymes »

Product Specifications

Source

Human embryonic kidney cell, HEK293-derived human Galectin-9 protein
Met1-Thr323

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met1 & Phe3

Predicted Molecular Mass

36 kDa

SDS-PAGE

42-51 kDa, reducing conditions

Activity

Measured by its ability of the immobilized protein to support the adhesion of Jurkat human acute T cell leukemia cells.
The ED50 for this effect is 0.75-4.5 μg/mL.

Reviewed Applications

Read 1 review rated 4 using 9064-GA in the following applications:

Scientific Data Images for Recombinant Human Galectin-9 Protein, CF

Recombinant Human Galectin-9 Protein Bioactivity

Recombinant Human Galectin-9 Protein Bioactivity

Recombinant Human Galectin-9 supports the adhesion of Jurkat human acute T cell leukemia cells. The ED50 for this effect is 0.75-4.5 μg/mL.

Formulation, Preparation and Storage

9064-GA
Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, NaCl, EDTA, DTT and Trehalose.
Reconstitution
Reconstitute at 200 μg/mL in PBS.

Reconstitution Buffer Available:
Size / Price
Qty
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.
  • 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.

Background: Galectin-9

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: prototype (one CRD), tandem-repeat (two CRDs), and chimeric (one CRD, unique N-terminus) (1, 2). Full length Galectin-9 is a widely expressed 39 kDa tandem-repeat Galectin that contains two CRDs connected by a linker region (3). Progressive deletion within the linker region generates a 36 kDa isoform, also known as Ecalectin or UAT, as well as a 35 kDa isoform (4). This recombinant protein corresponds to the Ecalectin isoform of human Galectin-9 and shares 70% and 73% aa sequence identity with the corresponding regions of mouse and rat Galectin-9, respectively. Galectin-9 exhibits a wide range of activities. All three isoforms function as eosinophil chemoattractants (5, 6). This activity is destroyed by thrombin-mediated cleavage within the linker region of the long isoform, although the Ecalectin isoform is resistant to thrombin (7). Galectin-9 binds to carbohydrate moieties of IgE, thereby preventing immune complex formation, mast cell degranulation, and asthmatic and cutaneous anaphylaxis reactions (8). Independent of its lectin properties, Galectin-9 induces the maturation of dendritic cells which promote Th1 polarization (9). Galectin-9 induces cellular apoptosis in part by direct binding to TIM-3 (10, 11). Its interaction with TIM-3 inhibits Th1 cell and CD8+ cytotoxic T cell responses and also promotes regulatory T cell differentiation and activity (11, 12). Galectin-9 suppresses tumor cell metastasis by interfering with the associations between hyaluronic acid and CD44 and between VCAM-1 and Integrin alpha4 beta1 (13). The Ecalectin isoform (UAT; urate transporter) can also be expressed as an integral membrane protein and mediate the cellular efflux of urate (14).

References

  1. Heusschen, R. et al. (2013) Biochim. Biophys. Acta 1836:177.
  2. Elola, M. T. et al. (2007) Cell. Mol. Life Sci. 64:1679.
  3. Tureci, O. et al. (1997) J. Biol. Chem. 272:6416.
  4. Chabot, S. et al. (2002) Glycobiology 12:111.
  5. Matsumoto, R. et al. (2002) J. Immunol. 168:1961.
  6. Sato, M. et al. (2002) Glycobiology 12:191.
  7. Nishi, N. et al. (2006) Glycobiology 16:15C.
  8. Niki, T. et al. (2009) J. Biol. Chem. 284:32344.
  9. Dai, S.-Y. et al. (2005) J. Immunol. 175:2974.
  10. Seki, M. et al. (2007) Arthritis Rheum. 56:3968.
  11. Zhu, C. et al. (2005) Nat. Immunol. 6:1245.
  12. Sehrawat, S. et al. (2010) PloS Pathogens 6:e1000882.
  13. Nobumoto, A. et al. (2008) Glycobiology 18:735.
  14. Leal-Pinto, E. et al. (2002) Am. J. Physiol. Renal Physiol. 283:F150.

Alternate Names

Ecalectin, GAL9, Galectin9, LGALS9

Entrez Gene IDs

3965 (Human); 16859 (Mouse)

Gene Symbol

LGALS9

UniProt

NP_002299

Additional Galectin-9 Products

Product Documents for Recombinant Human Galectin-9 Protein, CF

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Product Specific Notices for Recombinant Human Galectin-9 Protein, CF

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