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ZBiotech has developed a robust microarray platform that allows researchers to simultaneously profile glycosylation by multiple lectins. The lectin array utilizes a panel of 37 plant-based lectins for high-throughput glycosylation analysis. Each lectin has been validated by glycan microarrays to ensure binding specificity. The proprietary coating substrate of this array outperforms other substrates with exceptional sensitivity without compromising specificity. Each lectin array contains 8 or 16 identical subarrays, enabling the analysis of multiple samples simultaneously and facilitating rapid results in a simple and easy-to-use format. Varieties of biological samples can be analyzed by the array. For example, proteins, antibodies, cells, cell lysate, serum, vesicles, bacteria, and viral particles. The Lectin array can be customized to meet individual client needs. Assay services are available upon request.
Glycosylation is one of the most abundant posttranslational modifications in eukaryotic cells. It is a complex process in which multiple glycosyltransferases work together to covalently add carbohydrate structures to proteins, lipids, or ribonucleic acids. Glycosylation is an intracellular process essential to all eukaryotic cells. The carbohydrate structures stabilize proteins to ensure proper folding for optimal activities. They also involve cellular signaling regulation to enforce tissue homeostasis. Determining the chemistry and biology of glycosylation is indispensable for understanding the biology of living organisms.
The discovery of ricin by Stillmark in 1888 marked the beginning of lectinology, a discipline dedicated to studying lectins’ chemical and biological functions. In 1952, Watkins and Morgan found that adding sugars can block the agglutination of erythrocytes caused by lectins. This milestone discovery unveiled the carbohydrate-binding specificity of lectins. Since then, hundreds of lectins have been purified and studied from plants, microorganisms, and animals. Lectins are now defined as carbohydrate-binding proteins, and each lectin recognizes a unique repertoire of carbohydrate structures.
For example, SNA (Sambucus Nigra lectin), MAL1 (Maackia Amurensis Lectin I), and MAL2 (Maackia Amurensis Lectin II) are sialoglycan-specific lectins. SNA recognizes terminal α-2,6 sialic acids (either Neu5Ac or Neu5Gc). In stark contrast, MAL1 and MAL2 preferentially recognize terminal α-2,3 sialic acids (either Neu5Ac or Neu5Gc). Another example is Calsepa (Calystegia Sepium lectin). Calsepa generally binds with all N-linked glycans without differentiating a specific subtype of N-glycans with or without terminal sialic acids. Compared with Calsepa, BanLec (Musa Paradisiaca lectin) preferentially recognizes high-mannose N-glycans and hybrid N-glycans without terminal sialic acids.
Lectins have been widely used to detect glycosylation because of their unique carbohydrate-recognizing properties. ZBiotech has developed a robust microarray platform that allows researchers to simultaneously profile glycosylation by multiple lectins. The lectin array utilizes a panel of 37 plant-based lectins immobilized on the array surface for high-throughput glycosylation analysis. Each lectin has been validated by glycan microarrays to ensure binding specificity. The proprietary coating substrate of this array outperforms other substrates with exceptional sensitivity without compromising specificity. Each lectin array contains 8 or 16 identical subarrays, enabling the analysis of multiple samples simultaneously and facilitating rapid results in a simple and easy-to-use format. Varieties of biological samples can be analyzed by the array. For example, proteins, antibodies, cells, cell lysate, serum, vesicles, bacteria, and viral particles. The Lectin array can be customized to meet individual client needs. Assay services are available upon request.
Features
Applications
List of lectins and their binding specificities (download the PDF)
ID | Lectin | Binding Specificity |
---|---|---|
NL1 | AAL | Fucose-containing glycans; no binding to fucose on Blood Group A and B antigens except minor binding to type 2 antigens |
NL2 | AIA | O-glycans containing following motifs: T antigen (Core 1); Tn antigen; O-GalNAc Core 3; no binding to STn, Core 2, Core 4 and Core 6 O-GalNAc glycans, Blood Group ABH Antigens Type 3 |
NL3 | BC2L-C | Fucose; no or weak binding to Blood Group A and B type 2 antigens |
NL4 | BPL | Terminal β-Gal/β-GalNAc: PolyLacNAc > Mono/Di LacNAc. Sialic acid attached to Gal shields the binding. Fucose attached to GlcNAc allows the binding; no binding to Blood Group Antigens. |
NL5 | Calsepa | Bind to N-glycans; no difference between bisecting N-glycans, complex N-glycans and core-fucose N-glycans. |
NL6 | ConA | High-mannose, complex, hybrid, bisecting N-glycans; no binding to tri- and tetra-antennary N-glycans. |
NL7 | DBA | Glycans with Sda antigen motif (e.g., GM2); Blood Group A antigen |
NL8 | DSA | Type 2 LacNAc; (GlcNAcβ1-4)2 and some extended epitopes; bind to Blood Group antigen A, B, H, Type 2. |
NL9 | ECL | Terminal β1,4-Gal; no binding to Lewis X; bind to Blood Group Antigen H Type 2 |
NL10 | GNA | Exposed α1,3-Man on N-glycans |
NL11 | GSI-B4 | Terminal α1,3-Gal (or weaker α1,4-Gal); bind to Blood Group B Antigens |
NL12 | GSII | Terminal GlcNAc |
NL13 | HAA | Terminal α-GalNAc: Blood Group A > GalNAca1-3GalNAcb > All other α-GalNAc; Similar to HPA. |
NL14 | HHL | High Mannose N-glycans; Weak binding to Complex (non-bisecting GlcNAc) N-Glycans and other mannose polysaccharides; no binding to bisecting N-glycans. |
NL15 | HPA | Terminal GalNAc; weak binding to T antigen; no binding to Sda antigen, Blood Group A Antigen. Similar to HAA. |
NL16 | LCA | Core-fucose N-glycans; High-mannose N-glycans |
NL17 | LEL | LacNAc including Blood Group ABH antigens; weak binding to High-mannose N-glycans; α2,3-sialylated type 2 poly-LacNAc |
NL18 | LTA | Terminal Fucα1-3GlcNAc; Lewis X; Lewis Y; Blood Group H disaccharide, Type 2 and 6. |
NL19 | MAL-I | Terminal Neu5Ac(or Neu5Gc)α2-3Galβ1-4GlcNAc(or Glc), or 3′-sulfates; weak asialo partial-epitope binding; no binding to SLeX or Sda antigen |
NL20 | MAL-II | Terminal Neu5Ac(or Neu5Gc)α2-3Galβ1-4GlcNAc(or Glc), or 3′-sulfates; weak asialo partial-epitope binding; no binding to SLeX or Sda antigen |
NL21 | Morniga G | High-mannose N-glycan > Poly-LacNAc N-glycan > Tri-antennary N-glycans |
NL22 | NPA | High-mannose N-glycans > Hybrid N-glycans > Core-fucose N-glycans |
NL23 | PHA-E | Complex N-Glycans; no high-mannose binding |
NL24 | PHA-L | Bisecting N-glycans |
NL25 | PNA | Galβ1-3GalNAc (T antigen) |
NL26 | PSA | Core N-Glycan Fucose (Fuca1-6GlcNAc). No binding to non-fucosylated N-Glycans. |
NL27 | PTA | Bind to Blood Group H antigens except Type 1. |
NL28 | RCA-I | Terminal β1,4-Gal (β1,3 and β1,6 also accepted); no binding with terminal α2,3 sialic acid, or to T antigen or Lewis X; still binds to β1,4-Gal capped with terminal α2,6 sialic acid or 6′-sulfate. |
NL29 | RPA | Complex N-Glycans: Tetra-antennary > Tri-antennary; weak binding to Poly-LacNAc extended bi-antennary; no Other bi-antennary N-Glycan binding. |
NL30 | RSL | Fucose-containing glycans; includes all blood group fucose, core N-Glycan fucose ,and Lewis A/X Fucose |
NL31 | SBA | Terminal α-GalNAc or β-GalNAc; Tn antigen; MUC-1 glycopeptides; similar to VVL |
NL32 | SNA | Terminal Neu5Ac(or Neu5Gc)α2-6Galβ1-4; no asialo partial-epitope binding. |
NL33 | STL | Galβ1-4GlcNAc (type 2 poly-LacNAc) with weak partial-epitope binding; weak binding to High-mannose N-Glycans (GlcNAcB1-4GlcNAc epitope); bind to Blood Group ABH antigens type 2. |
NL34 | UEA-I | Fucα1-2Galβ1-4GlcNAc (Blood Group H Type 2, 5, 6, disaccharide); Lewis Y; α1,4-Fuc |
NL35 | VVL | Tn antigen; weak binding to blood group antigen A |
NL36 | WFA | Terminal GalNAc; terminal β-Gal on LacNAc; no binding to Lewis X. bind to Sda antigen; no T antigen binding. |
NL37 | WGA | GlcNAc; terminal and exposed α2,3-Neu5Ac; terminal and exposed α-GalNAc; no binding to Lewis X; no binding with terminal α2,6 sialic acid. |
Using lectin array to determine the binding specificity of mannan
Mannans are polymers containing mannose. The lectin array was assayed with biotinylated mannan (1 μg/mL), followed by streptavidin (Cy3). The array was scanned with a microarray scanner at 532nm wavelength. Positive control showed binding signals as expected. A few lectins, such as GNA, HHL, and NPA, bind to mannan. These lectins are known to interact with high-mannose N-glycans.
List of lectins and their binding specificities (download the PDF)
Protocol & User Manual (download the manual)