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G5170

Sigma-Aldrich

Galectin-3 human

recombinant, expressed in E. coli, lyophilized powder

Synonyme(s) :

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

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About This Item

Numéro MDL:
MFCD05665410
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

Produit recombinant

expressed in E. coli

Niveau de qualité

200

Forme

lyophilized powder

Numéro d'accès UniProt

P17931

Température de stockage

−20°C

Informations sur le gène

human ... LGALS3(3958)

Description générale

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

Actions biochimiques/physiologiques

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.

Autres remarques

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

Forme physique

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

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Matthew R Kovak et al.
American journal of reproductive immunology (New York, N.Y. : 1989), 72(4), 403-412 (2014-05-28)
Galectin-3 is a β-galactoside binding protein with immunomodulatory properties and exerts its extracellular functions via interactions with glycoconjugate ligands. Therefore, to elucidate the function of galectin-3, binding ligands in human seminal plasma were investigated. Galectin-3 binding proteins were isolated from
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
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)
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
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
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