Human LGALS8/mCherry Stable Cell Line-NCI-H358

LGALS8, also known as galectin-8 or Gal-8, is a member of the galectin family encoded by the LGALS8 gene located on human chromosome 1q43. Galectins are beta-galactoside-binding animal lectins characterized by conserved carbohydrate recognition domains, and they participate in a broad range of biological processes including cell-cell adhesion, cell-matrix interaction, growth regulation, apoptosis, RNA splicing, and immune modulation. Galectin-8 is unique among galectins for its tandem-repeat structure containing two distinct carbohydrate recognition domains connected by a linker peptide, allowing it to cross-link glycoproteins on the cell surface and within the extracellular matrix. The protein is widely expressed in normal tissues and is frequently upregulated in various tumor types, where it has been implicated in cancer cell invasion, metastasis, and modulation of the tumor microenvironment. The Human LGALS8/mCherry Stable Cell Line-NCI-H358 is a genetically engineered derivative of the NCI-H358 cell line, a well-characterized human non-small cell lung carcinoma line originally isolated from a male patient with minimally invasive lung adenocarcinoma. In this stable cell line, the full-length human LGALS8 coding sequence is fused in-frame with the mCherry fluorescent reporter gene and integrated into the host genome, allowing constitutive expression of the LGALS8-mCherry fusion protein under the control of a strong promoter.

This stable cell line offers a versatile tool for cancer research, particularly for studying the subcellular localization, trafficking, and dynamic behavior of galectin-8 in live lung cancer cells using fluorescence microscopy and high-content imaging. The mCherry tag enables direct visualization of LGALS8 without the need for antibody-based detection, facilitating real-time tracking of the protein during cell adhesion, migration, and invasion assays. Researchers can also use this cell line to investigate galectin-8 involvement in autophagy, particularly its role as a damage sensor for phagosomal and endosomal membranes during bacterial infection or cellular stress, as galectin-8 is known to recruit selective autophagy receptors such as NDP52 and TAX1BP1 to damaged vesicles. Additionally, the line can be employed in protein-protein interaction studies through co-immunoprecipitation or proximity ligation assays, leveraging the mCherry tag for pull-down or fluorescence-based detection. The stable expression ensures consistent and reproducible results across experiments, making it suitable for drug screening efforts aimed at identifying compounds that modulate galectin-8 function, expression, or localization.