Recombinant human Galectin-1/LGALS1 protein

Galectin-1 is a member of the beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. This protein is an autocrine negative growth factor that regulates cell proliferation. It controls cell survival by inducing apoptosis of activated T cells and immature thymocytes, thus Galectin-1 has immunosuppressive and anti-inflammatory properties. Galectin-1 also regulates tumor angiogenesis and is a target for angiostatic cancer therapy. Recombinant human Galectin-1 was expressed in E. coli and purified by using conventional chromatography

Product Specifications

Product Name Alternative

Gal-1, 14 kDa laminin-binding protein, HLBP14, 14 kDa lectin, Beta-galactoside-binding lectin L-14-I, Galaptin, HBL, HPL, Lactose-binding lectin 1, Lectin galactoside-binding soluble 1, Putative MAPK-activating protein PM12, S-Lac lectin 1, GBP

Expression System

E.coli

Antigen Species

Human

Tag

Non-Tagged

Applications

SDS-PAGE

Concentration

1 mg/mL (determined by Bradford assay)

Endotoxin

< 1 EU per 1ug of protein (determined by LAL method)

Purity

> 90% by SDS-PAGE

Molecular Weight

14.7 kDa (135aa) confirmed by MALDI-TOF

Additionnal Information

Galectin1, GAL1, GBP, LGALS1, S-Lac lectin1, galaptin, lactose-binding lectin 1, 14 kDa lectin, Beta galactoside binding lectin, Beta galactoside binding lectin L 14 I, DKFZp686E23103, Galectin, Galectin1, GBP, HBL, HPL, Lactose binding lectin 1, MAPK activating protein MP12, Lectin galactoside binding soluble 1, LGALS 1, Putative MAPK activating protein MP12, S Lac lectin 1., ATGP0385-10 µg, ATGP0385-20 µg, ATGP0385-50 µg, ATGP0385-100 µg, ATGP0385-250 µg, ATGP0385-500 µg, ATGP0385-1 mg, ATGP0385-10, ATGP0385-20, ATGP0385-50, ATGP0385-100, ATGP0385-250, ATGP0385-500, ATGP0385-1

References & Citations

Robert Kiss., et al. (2006) . Glycobiology. 6 (11) :137R-157R; ; Poirier F., et al. (2009) . Dev Growth Differ. 51 (7) :607-15.;

Other References

Suzuki O et al., Galectin-1-mediated cell adhesion, invasion and cell death in human anaplastic large cell lymphoma: Regulatory roles of cell surface glycans. (Int J Oncol. 2014) {https://pubmed.ncbi.nlm.nih.gov/24589677/}; ; Suzuki O et al., Sialylation and glycosylation modulate cell adhesion and invasion to extracellular matrix in human malignant lymphoma: Dependency on integrin and the Rho GTPase family. (Int J Oncol. 2015) {https://pubmed.ncbi.nlm.nih.gov/26497328/}; ; Campanero-Rhodes M.A et al., Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures. (Biomolecules. 2021) {https://pubmed.ncbi.nlm.nih.gov/33919637/}; ; Fabregat FN et al., Structure of the Lipopolysaccharide from Paenalcaligenes hominis: A Chemical Perspective on Immune Recognition. (JACS Au. 2025) {https://doi.org/10.1021/jacsau.5c00441}