LGALS3 Human

Galectin-3 Human Recombinant
Cat. No.
BT10696
Source
Escherichia Coli.
Synonyms
Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

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.  

Product Specs

Introduction
Galectin-3, in conjunction with the alpha-3, beta-1 integrin, facilitates cspg4-mediated stimulation of endothelial cell migration. This protein plays a crucial role in the development of vasculogenic mimicry and angiogenic properties observed during melanoma progression. LGALS3, encoding Galectin-3, exhibits high expression levels in early-stage papillary carcinoma, with its expression intensity decreasing as the tumor progresses. Elevated serum levels of LGALS3 are associated with thyroid malignancy. However, there is a significant overlap in serum LGALS3 concentrations between individuals with benign and malignant nodular thyroid disease. Functioning as an immune regulator, LGALS3 suppresses T-cell immune responses, thereby promoting tumor growth and contributing to tumor immune tolerance.
Description
Recombinant LGALS3, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 250 amino acids with a molecular weight of 26.2 kDa. The purification process involves proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The Galectin-3 protein was lyophilized from a sterile 0.2 micron filtered solution containing 10 mM sodium phosphate and 50mM sodium chloride at a pH of 7.5.
Solubility
Reconstitute the lyophilized LGALS3 in sterile 18MΩ-cm H2O to a concentration of at least 100 µg/ml. This solution can be further diluted in other aqueous solutions.
Stability
Lyophilized Galectin-3 Recombinant remains stable at room temperature for up to 3 weeks. However, it is recommended to store the lyophilized protein desiccated at a temperature below -18°C. After reconstitution, Galectin-3 should be stored at 4°C for 2-7 days. For long-term storage, store below -18°C. It is advisable to add a carrier protein (0.1% HSA or BSA) for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is greater than 95.0% as determined by SDS-PAGE analysis.
Synonyms
Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.
Source
Escherichia Coli.
Amino Acid Sequence

MADNFSLHDAL SGSGNPNPQG WPGAWGNQPA GAGGYPGASY PGAYPGQAPP GAYPGQAPPG AYPGAPGAYP GAPAPGVYPG PPSGPGAYPS SGQPSATGAY PATGPYGAPA GPLIVPYNLP LPGGVVPRML ITILGTVKPN ANRIALDFQR GNDVAFHFNP RFNENNRRVI VCNTKLDNNW GREERQSVFP FESGKPFKIQ VLVEPDHFKV AVNDAHLLQY NHRVKKLNEI SKLGISGDID LTSASYTMI.

Product Science Overview

Structure and Function

Galectin-3 is characterized by a carbohydrate recognition domain (CRD) that allows it to bind to beta-galactoside residues. This binding capability is crucial for its role in various biological processes. The protein is composed of 250 amino acids and has a molecular weight of approximately 26-31 kDa .

Biological Roles

  1. Cell Adhesion and Migration: Galectin-3 plays a significant role in cell adhesion and migration by interacting with cell surface glycoproteins. This interaction is essential for processes such as wound healing and immune cell trafficking .

  2. Apoptosis Regulation: Galectin-3 has anti-apoptotic properties, meaning it can prevent programmed cell death. This function is particularly important in cancer cells, where overexpression of Galectin-3 can contribute to tumor progression and metastasis .

  3. Immune Response: Galectin-3 is involved in modulating the immune response. It can influence the activity of various immune cells, including macrophages and T-cells, thereby playing a role in inflammation and immune regulation .

Recombinant Production

Recombinant human Galectin-3 is produced using various expression systems, including Escherichia coli (E. coli) and human embryonic kidney (HEK293) cells. The recombinant protein is often used in research to study its biological functions and potential therapeutic applications .

  1. E. coli Expression System: In this system, the human Galectin-3 gene is inserted into a plasmid vector, which is then introduced into E. coli cells. The bacteria express the protein, which is subsequently purified. This method is cost-effective and allows for high-yield production .

  2. HEK293 Expression System: This system involves the use of human cells to produce the recombinant protein. The HEK293 cells are transfected with the Galectin-3 gene, leading to the expression of the protein in a more native form. This method is often preferred for applications requiring high biological activity and proper post-translational modifications .

Applications

Recombinant human Galectin-3 is widely used in various research areas, including:

  1. Cancer Research: Due to its role in apoptosis and tumor progression, Galectin-3 is a target for cancer research. Studies focus on understanding its function in cancer cells and developing potential therapeutic strategies .

  2. Immunology: Galectin-3’s involvement in immune regulation makes it a valuable tool for studying immune responses and developing immunotherapies .

  3. Cell Biology: Researchers use recombinant Galectin-3 to study cell adhesion, migration, and other cellular processes, providing insights into fundamental biological mechanisms .

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