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G5170

Sigma-Aldrich

Galectin-3 human

recombinant, expressed in E. coli, lyophilized powder

Sinónimos:

CBP 35, Carbohydrate-binding protein 35, Gal-3, Galactose-specific lectin 3, Galactoside-binding protein

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About This Item

MDL number:
MFCD05665410
UNSPSC Code:
12352202
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

200

form

lyophilized powder

UniProt accession no.

P17931

storage temp.

−20°C

Gene Information

human ... LGALS3(3958)

General description

Galectin-3 protein comprises a N-terminal flexible domain and a C-terminal carbohydrate-recognition domain (CRD). It is mapped to human chromosome 14q22.3. Galectin-3 is expressed in sensory neurons, immune endothelial and epithelial cells.

Application

Galectin-3 human has been used:
  • to test its interaction with N-acetyl lactosamine coated onto quantum dots
  • to optimize Gal3-induced hemagglutination measurements in non-agglutinated or agglutinated chicken red blood cells (RBCs)
  • in Gal-3 binding assay of serum samples from multiple sclerosis patients

Biochem/physiol Actions

Galectin-3 (Gal3) has anti-apoptotic property and mediates adhesion of cancer cells to endothelium. The activity of Gal3 is inhibited by lactose. High levels of Gal3 is associated with cardiovascular disease and is a potential biomarker in fibrosis and inflammation associated with heart failure. Gal3 is involved in variety of biological events from differentiation to host defense and immunomodulation. Gal3 gene deletion is correlated to renal function anomalies like nephropathy. It is implicated in the pathogenesis of retinopathy and non-alcoholic fatty liver disease (NAFLD).
Galectin-3 has been associated with the inhibition of apoptosis and the progression of cancer, as well as being a mediator of inflammation. Studies have found a positive correlation between the expression of galectin-3 and tumorigenicity and metastasis in colon, liver, and thyroid cancer.

Other Notes

Galectin-3 is a member of the family of animal lectins, which selectively binds β-galactoside residues.

Physical form

The product is lyophilized from water with 2 μg of lactose as stabilizer per μg of galectin-3.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Synthesis of multivalent N-acetyl lactosamine modified quantum dots for the study of carbohydrate and galectin-3 interactions
Yang Y, et al.
Tetrahedron, 68(35), 7148-7154 (2012)
Wei Zhao et al.
Analytical biochemistry, 571, 37-39 (2019-02-25)
Hemagglutination inhibition (HAI) assay is a simple method quantifying relative binding activities of glycan-lectin interactions. Currently, interpretation of HAI data remains a manual task depending on visual observation. In this study we developed a digital data reading method for HAI
Rui Dong et al.
International journal of molecular medicine, 41(2), 599-614 (2017-12-06)
Galectin-3 is a member of the galectin family, which are β‑galactoside‑binding lectins with ≥1 evolutionary conserved carbohydrate‑recognition domain. It binds proteins in a carbohydrate‑dependent and ‑independent manner. Galectin‑3 is predominantly located in the cytoplasm; however, it shuttles into the nucleus
Giuseppe Pugliese et al.
Glycobiology, 25(2), 136-150 (2014-10-12)
Galectin-3 has been increasingly recognized as an important modulator of several biological functions, by interacting with several molecules inside and outside the cell, and an emerging player in numerous disease conditions. Galectin-3 exerts various and sometimes contrasting effects according to
Andrea Robotti et al.
Electrophoresis, 31(17), 2882-2893 (2010-08-18)
Plasma acute-phase proteins (APPs) glyco-isoforms are important biomarkers of inflammatory processes such as those occurring in multiple sclerosis (MS). Specific analysis of these proteins is often hampered by sample biochemical complexity. The aim of our study was to set up
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