LGALS1 Human

Galectin-1 Human Recombinant

LGALS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 135 amino acids and having a molecular mass of 14.7kDa.
The LGALS1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9991
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

LGALS1 Mouse

Galectin-1 Mouse Recombinant

LGALS1 mouse Recombinant produced E. coli is a single polypeptide chain containing 159 amino acids (1-135) and having a molecular mass of 17kDa.
LGALS1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10089
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

LGALS10 Human

Charcot-Leyden Crystal Protein Human Recombinant

LGALS10 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (1-142 a.a.) and having a molecular mass of 18.6kDa.
LGALS10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10160
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

LGALS13 Human

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.

Shipped with Ice Packs
Cat. No.
BT10237
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

LGALS14 Human

Galectin-14 Human Recombinant

LGALS14 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 162 amino acids (1-139 a.a.) and having a molecular mass of 18.5kDa. The LGALS14 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10307
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

LGALS16 Human

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.

Shipped with Ice Packs
Cat. No.
BT10378
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

LGALS2 Human

Galectin-2 Human Recombinant

LGALS2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids (1-132 a.a.) and having a molecular mass of 16.8 kDa. The LGALS2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10463
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

LGALS2 Mouse

Galectin-2 Mouse Recombinant

LGALS2 mouse Recombinant produced E. coli is a single polypeptide chain containing 153 amino acids (1-130) 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.
Shipped with Ice Packs
Cat. No.
BT10546
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

LGALS2 Mouse, Active

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.

Shipped with Ice Packs
Cat. No.
BT10635
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

LGALS3 Human

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.  

Shipped with Ice Packs
Cat. No.
BT10696
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Definition and Classification

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 .
Biological Properties

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 .

Biological Functions

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 .

Modes of Action

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 .

Regulatory Mechanisms

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 .

Applications

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 .

Role in the Life Cycle

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.

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