Galectin-8/LGALS8 (F9O3T) Rabbit mAb #45586
- WB
- IP
- IHC
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 32, 42 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
| Immunohistochemistry (Paraffin) | 1:50 - 1:200 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro176 of human Galectin-8/LGALS8 protein.
Background
Galectins are a family of β-galactose binding proteins with intracellular and extracellular activities regulating cell adhesion and migration, immune responses, inflammation, cell death, and proliferation and are linked to several pathological conditions (reviewed in 1). Galectins can be divided into three groups: 1) prototype galectins (Gal-1, -2, -5, -7, -10, -11, -13, and -16) having one carbohydrate-recognition domain (CRD); 2) tandem-repeat type galectins (Gal-4, -6, -8, -9, and -12) that have two CRDs joined by a linker peptide; and 3) a chimera-type (Gal-3) that has a single CRD joined to an N-terminal non-lectin domain.
Galectin-8 (Gal-8; gene name LGALS8), which belongs to the group of tandem-repeat galectins, is important in adaptive and innate immunity with significant roles in host defense as well as tumor progression (reviewed in 2,3). Extracellular galectin-8 promotes cell adhesion through interaction with several cell surface proteins, including integrins (4,5), CD44 (6), CD45 (7), and CD166 (8). Intracellular galectin-8 binds to farnesylated K-Ras4B, regulating MAPK signaling (9). It also exerts a role in xenophagy by binding to glycans exposed on bacterial pathogens and recruiting NDP52 for destruction by autophagy, thereby restricting bacterial proliferation (10,11). Abundant expression of galectin-8 has been observed in various cancer types and, in some cases, associated with poor prognosis (12-14).
- Johannes, L. et al. (2018) J Cell Sci 131, jcs208884. doi: 10.1242/jcs.208884.
- Purić, E. et al. (2024) Med Res Rev, doi: 10.1002/med.22041.
- Zick, Y. (2022) Biochem Soc Trans 50, 135-149.
- Cárcamo, C. et al. (2006) Exp Cell Res 312, 374-86.
- Hadari, Y.R. et al. (2000) J Cell Sci 113 ( Pt 13), 2385-97.
- Eshkar Sebban, L. et al. (2007) J Immunol 179, 1225-35.
- Tribulatti, M.V. et al. (2009) J Leukoc Biol 86, 371-80.
- Delgado, V.M. et al. (2011) FASEB J 25, 242-54.
- Meinohl, C. et al. (2019) Cancers (Basel) 12, 30. doi: 10.3390/cancers12010030.
- Thurston, T.L. et al. (2012) Nature 482, 414-8.
- Kim, B.W. et al. (2013) Nat Commun 4, 1613.
- Wang, Y. et al. (2023) Am J Cancer Res 13, 2517-2529.
- Gentilini, L.D. et al. (2017) Oncotarget 8, 44654-44668.
- Elola, M.T. et al. (2014) Histol Histopathol 29, 1093-105.
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