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Galactoagglutinin 1(LGALS1) is a β -galactoside binding lectin encoded by LGALS1 gene, which has both intracellular expression and extracellular secretion characteristics. It is mainly synthesized by tumor matrix fibroblasts, vascular endothelial cells and immunoregulatory cells, and can freely spread to extracellular matrix and local immune microenvironment. Compared with other members of the galectin family with different sugar chain binding preferences, LGALS1 only contains a single conserved carbohydrate recognition domain (CRD), which can specifically recognize and bind β -galactose modified glycoprotein on the surface of T cells, vascular endothelial cells and tumor cells. Under the physiological immune homeostasis, the basic secretion of LGALS1 can limit the overactivation of effector T cells, maintain peripheral autoimmune tolerance, and avoid abnormal activation of autoimmune. In the microenvironment of hypoxic solid tumor, tumor cells and stromal cells can significantly up-regulate the expression of LGALS1; LGALS1 secreted in large quantities can bind to glycosylated TCR and CD45 receptors on the surface of T cells, induce apoptosis of CD8⁺T cells, promote the migration of endothelial cells and drive the process of pathological angiogenesis. Other galectin can't compensate the broad-spectrum immunosuppression function of LGALS1 mediated by sugar chain, and extracellular LGALS1 targeted neutralization can effectively restore the body's anti-tumor cytotoxic immunity and inhibit angiogenesis. The abnormally high expression of LGALS1 will also aggravate the autoimmune tissue damage of chronic inflammatory lesions, making it an irreplaceable core target for tumor immune escape and anti-angiogenesis targeted screening.
LGALS1 can exert the regulation of intracellular and extracellular sugar binding at the same time, and rely on a single conservative CRD structure pocket to specifically recognize the β -galactose residue modified glycoprotein on the surface of immune cells and endothelial cells. Its haplotype sugar chain binding structure features and tandem repeat galectin form significant functional differentiation, giving it a unique broad-spectrum immunosuppression regulation ability. The glycoprotein cross-linking mechanism mediated by LGALS1 can effectively connect tumor hypoxia signal with adaptive immunosuppression pathway, and can dynamically balance physiological immune tolerance level and tumor pathological vascular progress according to tissue oxygen supply status. This molecule is widely involved in key physiological and pathological processes such as peripheral T cell homeostasis maintenance, tumor immune escape and pathological angiogenesis. Loss of LGALS1 function can significantly alleviate local immunosuppression and reshape the body's endogenous anti-tumor immune monitoring ability. To sum up, LGALS1 is the key target for the study of biological mechanism of soluble lectin and the research and development of tumor immune targeted therapy.
Fig. 1 Dual-group tumor progression schematic for studying Galectin-1 regulatory function in tumor-associated macrophage and CD8+ T cell immune crosstalk.1
The biological functions of monomeric LGALS1 lectin are fully focused on β-galactoside glycan recognition and tumor immune signal suppression:
Creative Biolabs offers high-quality LGALS1 proteins through optimized eukaryotic expression systems, including full-length wild-type LGALS1 and isolated carbohydrate recognition domain variants. These products retain native β-galactoside glycan binding biological activity, suitable for T cell apoptosis and angiogenic inhibitor screening assays. All LGALS1 proteins undergo strict quality control to ensure consistent performance and reliable application across diverse immunology research platforms.
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Creative Biolabs provides custom-engineered LGALS1 stable cell lines, including tumor stromal overexpression and blank empty vector control models. These cell lines are optimized for secreted lectin profiling and T cell suppressive signal functional analysis. Each cell line undergoes stringent validation to ensure stable expression profiles during long-term hypoxic cell culture, and can be widely deployed for large-scale tumor immunotherapy compound screening experiments.
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High-specificity recombinant antibodies targeting LGALS1 are developed via advanced antibody engineering technologies, with no cross-reactivity with other galectin paralog lectins. These antibodies are validated for intracellular and secreted LGALS1 tissue localization detection and tumor stroma expression profiling, and can be combined with CD8 T cell marker reagents to analyze immune suppressive lectin complexes in tumor microenvironment cell models.
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Beyond catalog products, Creative Biolabs offers specialized custom services for LGALS1 research:
LGALS1 is a soluble β-galactoside-binding lectin that binds T cell surface glycans to induce immune suppression and stimulate tumor angiogenesis.
Tumor-secreted LGALS1 is a major driver of anti-tumor immune evasion, a promising target for combinatory immunotherapy development.
No, all LGALS1 products and services are strictly for research use only, not intended for clinical diagnosis or human therapeutic trials.
Offerings include full-length secreted LGALS1 lectins, isoform-specific detection antibodies and custom stable cell lines for tumor immune research.
LGALS1 proteins are validated via β-galactoside glycan binding and T cell apoptotic functional testing.