Growth Factors
Product List
LGALS7 Human
Galectin-7 Human Recombinant
Recombinant Human Galectin-7, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 136 amino acids, resulting in a molecular weight of 15kDa. The purification of LGALS7 is achieved through proprietary chromatographic techniques.
LGALS2 Mouse, Active
Galectin-2, BioActive Mouse Recombinant
Recombinant Mouse LGALS2, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein contains 153 amino acids (including a 23 amino acid His-tag at the N-terminus, spanning residues 1-130 of the LGALS2 sequence) and has a molecular weight of 17.3 kDa. The protein is purified using proprietary chromatographic techniques.
LGALS3 Human
Galectin-3 Human Recombinant
LGALS3 Human, His
Galectin-3 Human Recombinant, His Tag
LGALS3 Mouse
Galectin-3 Mouse Recombinant
LGALS3 Mouse, Active
Galectin-3 Mouse Recombinant, BioActive
This product consists of recombinant LGALS3 protein derived from mice and produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 287 amino acids (specifically, amino acids 1 to 264), resulting in a molecular mass of 29.8 kDa. The LGALS3 protein is fused to a 23 amino acid His-tag at its N-terminus. Purification is achieved using proprietary chromatographic methods.
LGALS4 Human
Galectin-4 Human Recombinant
LGALS7 Human, His
Galectin-7 Human Recombinant, His Tag
LGALS7 Mouse
Galectin-7 Mouse Recombinant
LGALS14 Human
Galectin-14 Human Recombinant
Introduction
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:
- Prototypical Galectins: Homodimers consisting of two identical subunits (e.g., Galectin-1, -2, -5, -7, -10, -11, -14, -15).
- Tandem Repeat Galectins: Contain at least two distinct carbohydrate recognition domains (CRDs) within one polypeptide (e.g., Galectin-4, -6, -8, -9, -12).
- Chimeric Galectins: Only Galectin-3 in vertebrates, which can exist as a monomer or in a multivalent form .
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.
