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Glycan-related Reagents for Extracellular Vesicle (EV) Research

Extracellular Vesicles and Glycans

Extracellular Vesicles (EVs) are small vesicles with lipid bilayer that are secreted from various cells under physiological and pathological conditions and exist in the body fluids and cell culture supernatant. EVs include subtypes such as exosomes and microvesicles. EVs contain nucleic acids and proteins, and act as mediators of intercellular communication by entering the target cells. They are involved in many physiological responses and diseases, including cell differentiation, immune responses, infection, cancer, cardiovascular diseases, and neurodegeneration. EVs derived from mesenchymal stem cells are known to have therapeutic potential, with several clinical trials ongoing. EV applications to drug delivery platforms have also been developed.1,2)
Glycans exist not only on the surface of cells, but also on the surface of sEVs (small Extracellular Vesicles: EVs <200 nm in diameter) as glycoproteins or glycolipids.3) Importance of glycans on EVs has been shown. For example, glycocalyx on the cancer cell-derived EVs has been reported to involve in organotropic determination in cancer metastases.4) Glycans on the EV have been reported to play important role in the tuning of EV uptake.5)
TCI has many products related to glycans expressed on the EVs.

Extracellular Vesicles and Glycans

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Anti-glycolipid Antibodies

Antibodies are proteins which are one of the components of the immune system. The specificity of antibodies is likened to the interaction between a key and a keyhole. Anti-glycolipid antibodies can specifically recognize glycolipids. We mainly produce antibodies against glycolipids; Ganglio-series, Globo-series, Lacto-series, and Neolacto-series. These antibodies can be used for immunohistochemistry, cell-staining, flow cytometry, ELISA, TLC-immunostaining and other methods. Our antibodies are very useful tools for analyzing the expression of carbohydrate chains and their functions.


Anti-glycolipid Antibodies


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Lectins

Lectins are highly specific carbohydrate-binding proteins of nonimmune origin. Due to their ability to bind with cell-surface glycoproteins and glycolipids, lectins could agglutinate cells; they also could reversibly associate polysaccharides and glycoproteins in solution. Lectin has long been well-known as tools for detection and analysis of functional oligosaccharides in the glycoscience field. Recombinant lectins show better stability compared with lectins extracted from natural resources. TCI offers not only recombinant lectins but also chemically modified lectins such as several types of biotinylated lectin and lectin-agarose for detection and capturing of glycoconjugates.


LecBeads (Lectin-Agarose)

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Lectin-Biotin Conjugates

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Lectins

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Endoglycosidases

Endoglycoceramidase (EGCase) is a glycolipid-specific hydrolase that cleaves the glycosidic linkage between oligosaccharide and ceramide of various glycosphingolipids (GSLs). Recombinant EGCase (rEGCase) is activated under a detergent-dependent condition. In contrast, Activator II is capable of inducing activity of EGCases without any detergent reagents. By the use of Activator II, GSLs on cell surfaces of living cells could be hydrolyzed without cell disruption caused by detergent.​
On the other hand, Endo-M is one of the enzymes known as endo-β-N-acetylglucosaminidases (endo-β-GlcNAc-ases). This enzyme was found by Yamamoto et al.,7) in the culture fluid of Mucor hiemalis isolated from soil. Endo-M hydrolyzes the N,N'-diacetylchitobiose moiety in oligosaccharides bound to the asparaginyl residue of various glycoproteins through the N-glycosidic linkage. The efficacy of this enzyme comes from the fact that one N-acetylglucosamine residue remains bound to the protein while cleaving the N,N'-diacetylchitobiose moiety. The enzyme is thus able to transfer the intact oligosaccharide to suitable acceptors. These endoglycosidases are expected to be used for the analysis of sugar chain structures and sugar chain functions on extracellular vesicles.


Endoglycosidases


Endoglycosidases and Related Enzymes

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References

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