Galectin-9 (D9R4A) XP® Rabbit mAb (BSA and Azide Free) #71325
- WB
- IHC
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 9-40 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.
Formulation
For standard formulation of this product see product #54330
Storage
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Background
Galectin-9 is induced by proinflammatory stimuli, including IFN-γ, TNF-α, and TLR ligands, and regulates various immune responses through interaction with its ligand TIM-3 (8, 9). Binding of galectin-9 to TIM-3 expressed by Th1 CD4 T cells resulted in T cell death (9). On the other hand, galectin-9 treatment of tumor-bearing mice increased the number of IFN-γ-producing TIM-3+ CD8 T cells and TIM-3+ dendritic cells (10). Transgenic overexpression of either TIM-3 or galectin-9 in mice led to an increase in cells with a myeloid-derived suppressor cell phenotype and inhibition of immune responses (11). CD44 is also proposed to be a receptor for galectin-9, and interaction of galectin-9 with CD44 expressed by induced regulatory T (iTreg) cells enhanced the stability of function of iTreg cells. In addition, galectin-9 was recently demonstrated to bind Dectin-1 expressed by pancreatic ductal adenocarcinoma-infiltrating macrophages, resulting in tolerogenic macrophage reprogramming and suppression of anti-tumor immunity. Increased galectin-9 expression has been observed in several cancer types, including lung, liver, breast, and kidney (12). Alternative splicing of the galectin-9 transcript leads to several isoforms (13).
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- Barondes, S.H. et al. (1994) J Biol Chem 269, 20807-10.
- Offner, H. et al. (1990) J Neuroimmunol 28, 177-84.
- Wells, V. and Mallucci, L. (1991) Cell 64, 91-7.
- Filer, A. et al. (2009) Arthritis Rheum 60, 1604-14.
- Perillo, N.L. et al. (1995) Nature 378, 736-9.
- Cooper, D.N. et al. (1991) J Cell Biol 115, 1437-48.
- Gieseke, F. et al. (2013) Eur J Immunol 43, 2741-9.
- Zhu, C. et al. (2005) Nat Immunol 6, 1245-52.
- Nagahara, K. et al. (2008) J Immunol 181, 7660-9.
- Dardalhon, V. et al. (2010) J Immunol 185, 1383-92.
- Heusschen, R. et al. (2014) Biochim Biophys Acta 1842, 284-92.
- Heusschen, R. et al. (2013) Biol Reprod 88, 22.
Limited Uses
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