Human Galectin-9 Antibody Summary
Met1-Thr323
Accession # NP_002299
Applications
This antibody functions as an ELISA capture antibody when paired with Mouse Anti-Human Galectin‑9 Monoclonal Antibody (Catalog # MAB20452).
This product is intended for assay development on various assay platforms requiring antibody pairs. We recommend the Human Galectin-9 DuoSet ELISA Kit (Catalog # DY2045) for convenient development of a sandwich ELISA or the Human Galectin-9 Quantikine ELISA Kit (Catalog # DGAL90) for a complete optimized ELISA.
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
Human Galectin‑9 ELISA Standard Curve. Recombinant Human Galectin-9 protein was serially diluted 2-fold and captured by Mouse Anti-Human Galectin-9 Monoclonal Antibody (Catalog # MAB20451) coated on a Clear Polystyrene Microplate (Catalog # DY990). Mouse Anti-Human Galectin-9 Monoclonal Antibody (Catalog # MAB20452) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998) followed by Substrate Solution (Catalog # DY999) and stopping the enzymatic reaction with Stop Solution (Catalog # DY994).
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-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 alpha 4 beta 1 (13). The Ecalectin isoform (UAT; urate transporter) can also be expressed as an integral membrane protein and mediate the cellular efflux of urate (14).
- Yang, R-Y. et al. (2008) Expert Rev. Mol. Med. 10:e17.
- Elola, M. T. et al. (2007) Cell. Mol. Life Sci. 64:1679.
- Tureci, O. et al. (1997) J. Biol. Chem. 272:6416.
- Chabot, S. et al. (2002) Glycobiology 12:111.
- Matsumoto, R. et al. (2002) J. Immunol. 168:1961.
- 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.
- 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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