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Glycosphingolipid (GSL) glycan microarray technology is developed to allow researchers to explore the interactions between GSL glycans and biological samples such as proteins, antibodies, cells, cell lysate, serum, vesicles, bacteria, or viral particles. The GSL glycan array features 58 distinct GSL glycan structures. Each array contains 8 or 16 identical subarrays, enabling the simultaneous analysis of multiple samples. The GSL glycan array provides high-throughput and reliable glycan-binding information with a simple assay format that only requires a small sample volume. It can be customized to meet individual client needs. Assay services are available upon request.
Glycosphingolipids (GSLs), a subclass of glycolipids, are central components of the cellular membrane. A GSL molecule comprises a hydrophobic ceramide backbone covalently linked to a hydrophilic glycan moiety. The glycan moieties are either neutral, sialylated, or sulfated. Glycan portions of GSLs can be further classified based on the sequence and configuration of the sugar moieties into globo-, lacto-, neoLacto-, and ganglioside types of GSL glycans. These glycan structures are linked to various ceramides, creating structurally diversified GSLs.
In normal physiological conditions, GSL glycans play diverse roles in maintaining membrane structure, transducing cellular signals, and providing scaffolds for cell-to-cell interactions. However, abnormal presentations of these glycans have been linked to metabolic diseases, cancer, and neurodegenerative diseases. For example, the aberrant expression of specific GSL glycans is a hallmark of cancer cells, altering a range of cellular functions to promote survival. Deregulation of GSL glycans also impacts neuroinflammation associated with Parkinson’s. Therefore, identifying and understanding the differences between GSL glycans expressed in normal and pathological conditions is vital for understanding the pathogenesis of these diseases.
GSL glycans have gained increasing interest in the biomedical research community. ZBiotech has developed a robust microarray platform that allows researchers to explore the interactions between GSL glycans and biological samples, such as proteins, antibodies, cells, cell lysate, serum, vesicles, bacteria, or viral particles. The GSL glycan array features 58 artificially synthesized GSL glycan epitopes immobilized on a solid array surface for binding analysis. It provides useful glycan-binding information for evaluating GSLs – based biological interactions. Each array contains 8 or 16 identical subarrays, enabling the simultaneous analysis of multiple samples. The GSL Glycan Array provides high-throughput and reliable glycan-binding information with a simple assay format that only requires a small sample volume. It can be customized to meet individual client needs. Assay services are available upon request.
Features
Applications
List of GSL glycan structures on the array (download the PDF)
Type | ID | Glycan Structure | Abbreviation |
---|---|---|---|
Ganglioside | G1 | Neu5Acα2–3Galβ1–4Glc | Ac-GM3 |
G2 | Neu5Gcα2–3Galβ1–4Glc | Gc-GM3 | |
G3 | Kdnα2–3Galβ1–4Glc | Kdn-GM3 | |
G4 | Neu5Ac8Meα2–3Galβ1–4Glc | Ac8Me-GM3 | |
G5 | Neu5Acα2–3(GalNAcβ1–4)Galβ1–4Glc | Ac-GM2 | |
G6 | Neu5Gcα2–3(GalNAcβ1–4)Galβ1–4Glc | Gc-GM2 | |
G7 | Kdnα2–3(GalNAcβ1–4)Galβ1–4Glc | Kdn-GM2 | |
G8 | Neu5Acα2–3(Galβ1–3GalNAcβ1–4)Galβ1–4Glc | Ac-GM1 | |
G9 | Neu5Gcα2–3(Galβ1–3GalNAcβ1–4)Galβ1–4Glc | Gc-GM1 | |
G10 | Kdnα2–3(Galβ1–3GalNAcβ1–4)Galβ1–4Glc | Kdn-GM1 | |
G11 | Neu5Acα2–8Neu5Acα2–3Galβ1–4Glc | Ac-Ac-GD3 | |
G12 | Neu5Acα2–8Neu5Gcα2–3Galβ1–4Glc | Ac-Gc-GD3 | |
G13 | Neu5Acα2–8Kdncα2–3Galβ1–4Glc | Ac-Kdn-GD3 | |
G14 | Neu5Gcα2–8Neu5Acα2–3Galβ1–4Glc | Gc-Ac-GD3 | |
G15 | Neu5Gcα2–8Neu5Gcα2–3Galβ1–4Glc | Gc-Gc-GD3 | |
G16 | Kdnα2–8Neu5Acα2–3Galβ1–4Glc | Kdn-Ac-GD3 | |
G17 | Kdnα2–8Neu5Gcα2–3Galβ1–4Glc | Kdn-Gc-GD3 | |
G18 | Kdnα2–8Kdnα2–3Galβ1–4Glc | Kdn-Kdn-GD3 | |
G19 | Neu5Acα2–8Neu5Acα2–3(GalNAcβ1–4)Galβ1–4Glc | Ac-Ac-GD2 | |
G20 | Neu5Acα2–8Neu5Gcα2–3(GalNAcβ1–4)Galβ1–4Glc | Ac-Gc-GD2 | |
G21 | Neu5Gcα2–8Neu5Acα2–3(GalNAcβ1–4)Galβ1–4Glc | Gc-Ac-GD2 | |
G22 | Neu5Gcα2–8Neu5Gcα2–3(GalNAcβ1–4)Galβ1–4Glc | Gc-Gc-GD2 | |
G23 | Kdnα2–8Neu5Acα2–3(GalNAcβ1–4)Galβ1–4Glc | Kdn-Ac-GD2 | |
G24 | Kdnα2–8Neu5Gcα2–3(GalNAcβ1–4)Galβ1–4Glc | Kdn-Gc-GD2 | |
G25 | Kdnα2–8Kdnα2–3(GalNAcβ1–4)Galβ1–4Glc | Kdn-Kdn-GD2 | |
G26 | Neu5Acα2–3Galβ1–3GalNAcb1–4(Neu5Aca2–3)Galβ1–4Glc | Ac-Ac-GD1a | |
G27 | Neu5Acα2–8Neu5Acα2–3(Galβ1–3GalNAcβ1–4)Galβ1–4Glc | Ac-Ac-GD1b | |
G28 | Neu5Gcα2–8Neu5Gcα2–3(Galβ1–3GalNAcβ1–4)Galβ1–4Glc | Gc-Gc-GD1b | |
G29 | Kdnα2–8Neu5Gcα2–3(Galβ1–3GalNAcβ1–4)Galβ1–4Glc | Kdn-Gc-GD1b | |
G30 | Neu5Acα2–8Neu5Acα2–3Galβ1–3GalNAcβ1–4(Neu5Aca2–3)Galβ1–4Glc | Ac-Ac-Ac-GT1a | |
G31 | GalNAcβ1-4(Neu5Acα2–8Neu5Acα2–8Neu5Acα2–3)Galβ1–4Glc | Ac-Ac-Ac-GT2 | |
G32 | Neu5Acα2–8Neu5Acα2–8Neu5Acα2–3Galβ1–4Glc | Ac-Ac-Ac-GT3 | |
Lacto- and Neolacto-series | G33 | GlcNAcβ1–3Galβ1–4Glc | Lc3 |
G34 | Galβ1–3GlcNAcβ1–3Galβ1–4Glc | Lc4 (LNT) | |
G35 |
Galβ1–4GlcNAcβ1–3Galβ1–4Glc |
nLc4 (LNnT) | |
G36 | Galβ1–4(Fucα1–3)GlcNAcβ1–3Galβ1–4Glc | Fuc-nLc4 | |
G37 | Neu5Acα2–3Galβ1–4GlcNAcβ1–3Galβ1–4Glc | Ac-nLc4 | |
G38 | Neu5Gcα2–3Galβ1–4GlcNAcβ1–3Galβ1–4Glc | Gc-nLc4 | |
G39 | Kdnα2–3Galβ1–4GlcNAcβ1–3Galβ1–4Glc | Kdn-nLc4 | |
G40 | Neu5Ac8Meα2–3Galβ1–4GlcNAcβ1–3Galβ1–4Glc | 8MeAc-nLc4 | |
G41 | Neu5Acα2–3Galβ1–3GlcNAcβ1–3Galβ1–4Glc | Ac-Lc4 | |
G42 | Neu5Gcα2–3Galβ1–3GlcNAcβ1–3Galβ1–4Glc | Gc-Lc4 | |
G43 | Kdnα2–3Galβ1–3GlcNAcβ1–3Galβ1–4Glc | Kdn-Lc4 | |
G44 | Neu5Ac8Meα2–3Galβ1–3GlcNAcβ1–3Galβ1–4Glc | 8MeAc-Lc4 | |
G45 | Neu5Gcα2–3Galβ1–4(Fucα1–3)GlcNAcβ1–3Galβ1–4Glc | Gc-Fuc-nLc4 | |
G46 | Kdnα2–3Galβ1–4(Fucα1–3)GlcNAcβ1–3Galβ1–4Glc | Kdn-Fuc-nLc4 | |
Globo- and Isoglobo-series | G47 | Galα1–4Galβ1–4Glc | Gb3 |
G48 | Galα1–3Galβ1–4Glc | iGb3 | |
G49 | GalNAcβ1–3Galα1–4Galβ1–4Glc | Gb4 | |
G50 | GalNAcβ1–3Galα1–3Galβ1–4Glc | iGb4 | |
G51 | Galβ1–3GalNAcβ1–3Galα1–4Galβ1–4Glc | Gb5 (SSEA-3) | |
G52 | Galβ1–3GalNAcβ1–3Galα1–3Galβ1–4Glc | iGb5 | |
G53 | Fucα1-2Galβ1-3GalNAcβ1-3Galα1-4Galβ1-4Glc | Globo-H | |
G54 | Neu5Gcα2–3Galβ1–3GalNAcβ1–3Galα1–4Galβ1–4Glc | Gc-Gb5 | |
G55 | Kdnα2–3Galβ1–3GalNAcβ1–3Galα1–4Galβ1–4Glc | Kdn-Gb5 | |
G56 | Neu5Acα2–3Galβ1–3GalNAcβ1–3Galα1–3Galβ1–4Glc | Ac-iGb5 | |
G57 | Neu5Gcα2–3Galβ1–3GalNAcβ1–3Galα1–3Galβ1–4Glc | Gc-iGb5 | |
G58 | Kdnα2–3Galβ1–3GalNAcβ1–3Galα1–3Galβ1–4Glc | Kdn-iGb5 |
Using GSL glycan microarray to determine the binding specificity of Wisteria Floribunda Lectin (WFA)
The GSL glycan array was assayed with biotinylated Wisteria Floribunda Lectin (10 μg/mL), followed by streptavidin (Cy3). The array was scanned with a microarray scanner at 532nm wavelength. Positive control showed binding signals as expected. WFA binds to a series of GSL glycans (GM2 and GD2).
List of GSL glycan structures on the array (download the PDF)
Protocol & User Manual (download the manual)