LGALS1 Human

Galectin-1 Human Recombinant

Recombinant human LGALS1, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 135 amino acids, resulting in a molecular weight of 14.7 kDa. The purification of LGALS1 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9991
Source
Escherichia Coli.
Appearance
White, sterile-filtered powder obtained by lyophilization (freeze-drying).

LGALS1 Mouse

Galectin-1 Mouse Recombinant

Recombinant LGALS1 from mouse, produced in E. coli, is a single polypeptide chain of 159 amino acids (amino acids 1-135) with a molecular weight of 17 kDa. It includes a 24 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT10089
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

LGALS10 Human

Charcot-Leyden Crystal Protein Human Recombinant

Recombinant human LGALS10, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 162 amino acids (residues 1-142) with a molecular weight of 18.6 kDa. It includes a 20 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10160
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

LGALS8 Human

Galectin-8 Human Recombinant

Recombinant Human Galectin-8, expressed in E. coli, is a single, non-glycosylated polypeptide chain containing 317 amino acids. It has a molecular weight of 35.8 kDa. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11393
Source
Escherichia Coli.
Appearance
Sterile, white lyophilized powder.

LGALS8 Human, His

Galectin-8 Human Recombinant, His Tag

Recombinant human LGALS8, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 337 amino acids (specifically, amino acids 1-317) and exhibits a molecular weight of 37.9 kDa. This LGALS8 protein is engineered with a 20 amino acid His-Tag at its N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11469
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution that has been filtered for sterility.

LGALS8 Mouse

Galectin-8 Mouse Recombinant

Recombinant LGALS8, produced in E. coli, is a single polypeptide chain consisting of 339 amino acids (residues 1-316) and possessing a molecular weight of 38kDa. This protein is engineered with a 23 amino acid His-tag fused at its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11552
Source
Escherichia Coli.
Appearance
A sterile-filtered solution, clear and colorless.

LGALS9 Human

Galectin-9 Human Recombinant

Recombinant LGALS9, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 168 amino acids (1-148 a.a.). With a molecular weight of 18.5 kDa, this protein is fused to a 20-amino acid His-tag at its N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11597
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

LGALS9 Mouse

Galectin-9 Mouse Recombinant

Recombinant LGALS9 from mouse, produced in E. coli, is a single polypeptide chain consisting of 345 amino acids (residues 1-322) with a molecular weight of 38 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11659
Source
Escherichia Coli.
Appearance
Sterile, colorless solution that has been filtered.

LGALS13 Human

Galectin-13 Human Recombinant

Recombinant Human LGALS13, expressed in E. coli, is a single polypeptide chain without glycosylation, with a molecular weight of 16 kDa. It can exist as a homodimer, resulting in a total molecular weight of 32 kDa. A 6xHis tag is fused to the N-terminal of LGALS13, and it undergoes purification using standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT10237
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

LGALS4 Mouse

Galectin-4 Mouse Recombinant

Recombinant LGALS4 from mouse, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 349 amino acids (1-326a.a) with a molecular weight of 38.8 kDa. The protein includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT11025
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
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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