Galectin-1 Human Recombinant
Galectin-1 Mouse Recombinant
Charcot-Leyden Crystal Protein Human Recombinant
Galectin-13 Human Recombinant
Recombinant Human LGALS13 produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 16kDa. The LGALS13 also might appear as a homodimer, having a total Mw of 32kDa. LGALS13 is fused to a 6xHis tag at n-terminal and purified using standard chromatography techniques.
Galectin-14 Human Recombinant
Galectin-16 Human Recombinant
LGALS16 Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 16kDa.
The LGALS16 also appears as a homodimer and therefore a 32kDa band is observed as well. LGALS16 is fused to a 6xHis tag at n-terminal and purified using standard chromatography techniques.
Galectin-2 Human Recombinant
Galectin-2 Mouse Recombinant
Galectin-2, BioActive Mouse Recombinant
LGALS2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (1-130 a.a) and having a molecular mass of 17.3kDa.
LGALS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Galectin-3 Human Recombinant
LGALS3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 250 amino acids and having a molecular mass of 26.2kDa. The LGALS3 is purified by proprietary chromatographic techniques.
Galectins are a family of carbohydrate-binding proteins that specifically bind to β-galactoside sugars, such as N-acetyllactosamine. They are also known as S-type lectins due to their dependency on disulfide bonds for stability and carbohydrate binding . There are about 15 galectins discovered in mammals, encoded by the LGALS genes, and they are numbered consecutively. Galectins are classified into three types based on their structure:
Galectins are involved in various physiological functions, such as inflammation, immune responses, cell migration, autophagy, and signaling . They are expressed in numerous cell types and tissues, including hepatocytes, activated macrophages, dendritic cells, bone marrow, and epithelial cells in the intestines and lungs . The expression pattern of galectins varies between cell types and tissues, and they can be found in the cytosol, nucleus, extracellular matrix, or in circulation .
Galectins play a crucial role in mediating cell-cell interactions, cell-matrix adhesion, and transmembrane signaling . They are involved in immune responses by modulating inflammation, cell migration, and pathogen recognition . Galectins can bind to both carbohydrate and non-carbohydrate ligands, serving as adaptors within the cell to recruit enzymes and regulate pre-mRNA splicing, mRNA stability, autophagy, and apoptosis .
Galectins function through carbohydrate-dependent and carbohydrate-independent interactions. They bind to glycosylated proteins and lipids on the surface of host cells and pathogens, forming signaling and adhesion networks . Intracellularly, galectins can tune kinase and G-protein-coupled signaling cascades important for nutrient sensing, cell cycle progression, and transformation . They also participate in pre-mRNA splicing in the nucleus and recruit components of autophagosomes during intracellular infection .
The expression and activity of galectins are regulated through transcriptional regulation and post-translational modifications. Glycosylation is a common post-translational modification process that affects galectin function . Galectins can regulate cell death both intracellularly and extracellularly by cross-linking glycans on the outside of cells and transducing signals across the membrane to trigger apoptosis . They also play a role in autophagy regulation and inflammasome-dependent cell death programs .
Galectins have significant applications in biomedical research, diagnostic tools, and therapeutic strategies. They are involved in immune and inflammatory responses, tumor development and progression, neural degeneration, atherosclerosis, diabetes, and wound repair . Galectin-3, in particular, has been studied for its role in cancer immunotherapy and overcoming tumor immune escape . Inhibition of galectins is being explored as a potential therapeutic approach in cancer treatment .
Galectins play a vital role throughout the life cycle, from development to aging and disease. They are involved in cell growth, differentiation, apoptosis, cell adhesion, chemoattraction, and cell migration . Galectins also participate in immune regulation, pattern recognition, and pathogenesis of autoimmune diseases and cancer . Their functions are essential for maintaining cellular homeostasis and responding to physiological and pathological conditions.