Galectin 9 Rabbit Monoclonal Antibody (Clone RM499)

Galectin 9 is a β-galactoside-binding protein encoded by the LGALS9 gene and a member of the galectin family.¹ It contains two non-identical carbohydrate recognition domains (CRDs) joined by a peptide linker, the length of which depends on alternative splicing of the LGALS9 gene, which produces a short, medium, or long variant of the protein.^1,2 The non-identical CRDs are responsible for binding to different types of saccharide ligands with the N-terminal CRD (NCRD) preferring more complex glycoconjugates.¹ Galectin 9 is localized to the cytosol, nucleus, and extracellular matrix and is expressed primarily in immune-related tissues and cells.³ When expressed on immune or tumor cells, galectin 9 binds to glycosylated sites on the immunoregulatory protein TIM-3 and activates signaling that impairs immune synapse formation leading to T cell anergy or apoptosis.⁴ It also binds to the transmembrane glycoprotein CD44 on osteoblasts, leading to their proliferation, and it has a role in cell adhesion by preventing hyaluronic acid from binding to CD44.⁵ It activates CD4⁺ T cell populations and induces naïve T cells to acquire a central memory T cell (T_CM) phenotype.⁶ Galectin 9 was originally identified as a tumor antigen in patients with Hodgkin’s disease.¹ It is expressed to a lower extent in tumor cells compared with non-tumor cells but is increased in leukemia and colon cancer cell lines.³ Cayman’s Galectin 9 Rabbit Monoclonal Antibody (Clone RM499) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.

WARNING This product is not for human or veterinary use.

1. Nagae, M., Nishi, N., Murata, T., et al. Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain from Mus musculus reveals the basic mechanism of carbohydrate recognition. The Journal of Biological Chemisty 281(47), 35884-35893 (2006).

2. Chabot, S., Kashio, Y., Seki, M., et al. Regulation of galectin-9 expression and release in Jurkat T cell line cells. Glycobiology 12(2), 111-118 (2002).

3. Heusschen, R., Griffioen, A.W., and Thijssen, V.L. Galectin-9 in tumor biology: A jack of multiple trades. Biochim. Biophys. Acta 1836(1), 177-185 (2013).

4. Wolf, Y., Anderson, A.C., and Kuchroo, V.K. TIM3 comes of age as an inhibitory receptor. Nat. Rev. Immunol. 20(3), 173-185 (2020).

5. John, S., and Mishra, R. Galectin-9: From cell biology to complex disease dynamics. J. Biosci. 41(3), 507-534 (2016).

6. Gooden, M.J.M., Wiersma, V.R., Samplonius, D.F., et al. Galectin-9 activates and expands human T-helper 1 cells. PLoS One 8(5), e65616 (2013).