Lectin microarray is a high-throughput technique used to analyze glycan patterns on glycoproteins by probing them with an array of immobilized lectins, each with specificity for different carbohydrate structures. Fluorescently labeled glycoproteins or samples are incubated on the microarray, and binding signals reveal the presence and abundance of specific glycan motifs.
We have over 15 years of experience in lectin microarray development and analysis of recombinant glycoproteins, serum glycoproteins, synthetic neoglycoproteins, cells, and exosomes
Our default setup:
48 highly purified lectins isolated from natural sources with well-established glycan binding specificities are printed in 5 replicates alongside control samples (printing buffer containing BSA). We print our lectin microarrays on Premium Schott Nexterion 3D hydrogel glass slides with an ultralow background and excellent protein stabilization properties.
| Type | Lectin | Specificity | Monosaccharide |
|---|---|---|---|
| AAA | Anguilla anguilla lectin | α-L-fucose | α-L-fucose |
| AAL | Aleuria Aurantia | Fuc | Fuc |
| ABL | Agaricus bisporus | Gal(β1-3)GalNAc, T antigen | Gal |
| ACA | Amarantus Caudatus | T antigen, (Galβ1-3GalNAcα-Thr/Ser) | Gal |
| AHP | Arachis hypogaea AHA | Gal(β1-3)GalNAc, T Antigen | Gal |
| AIA/JAC | Artocarpus integrifolia (Jacalin) | T antigen | GalNAc |
| AOL | Aspergillus orzyae | Fucose | Fuc |
| ASA | Allium sativum lectin | α1,3-mannose | Man |
| BPL | Bauhinia Purpurea | Galβ-1,3 or β1,4-GalNAc | Gal |
| BS-I/GS-I | Griffonia simplicifolia I | α-Gal | Gal |
| BS-II/GS-II | Griffonia simplicifolia II | Terminal GlcNAc | GlcNAc |
| CAL | Cicer arietinum | Fetuin, Lac, IgM | Lac |
| CFL | Codium fragile | GalNAc | GalNAc |
| ConA | Concanavalin A | α-Man, α-Glc | Man |
| DBL/DBA | Dolichos biflorus | α-GalNAc | GalNAc |
| DSL | Datura stramonium | (GlcNAc)2, LacNAc | GalNAc |
| ECA | Erythrina Cristagalli A | Gal, GalNac | GalNAc |
| EEA | Euonymus Europaeus | Lac, blood groups B and H | Gal |
| GNA | Galanthus Nivalis | terminal α1,-3Man | Man |
| HAL | Helix aspersa | GalNAc | GalNAc |
| HMA | Homarus americanus | LAg1: NeuNAc. LAg2: GalNAc | Sialic acid, GalNAc |
| HPL | Helix pomatia | α-GalNAc terminal | GalNAc |
| LBA | Phaseolus lunatus | GalNAc-α1,3[Fuc-α1,2]Gal | GalNac |
| LEL | Lycopersicon esculentum | (GlcNAc)3 | GlcNAc |
| LTL | Lotus tetragonolobus | Terminal α-Fuc, Lex | Fuc |
| MAL-I | Maackia amurensis Lectin I | α2,3-SialLacNac | Sial |
| MAL-II | Maackia amurensis Lectin II | LacNAc | Gal |
| MOA | Marasmium oreades agglutinin | Gal-α1,3-Gal and Gal-α1,3-Gal-β1,4-GlcNAc | α-Gal |
| MPA | Maclura Pomifera | T antigen, α-GalNAc | Gal |
| NPL | Narcissus Pseudonarcissus | Terminal and internal Man | Man |
| PAL | Pseudomonas aeruginosa PA-I | Gal | Gal |
| PHA E+L | Phaseolus Vulgaris Agglutining | oligomers | Lac |
| PNA | Peanut agglutinin | T antigen, Gal(β-1,3) GalNac | Gal |
| PSA | Pisum sativum | Fucα-1,6-GlcNAc and α-Man | Fuc |
| PT-I | Psophocarpus tetragonolobus I | α-GalNAc | GalNAc |
| PT-II | Psophocarpus tetragonolobus II | α-1,2-fucosylated LacNAc | Gal |
| PWA | Phytolacca americana | (GlcNAc)3 | GlcNAc |
| RCA120 | Ricinus Communis Agglutinin, | β-Gal, Lac, LacNAc | Gal |
| SBA | Soybean agglutinin | α-Gal-GalNAc | GalNAc |
| SJA | Sophora japonica | GalNAc | GalNAc |
| SNA | Sambucus nigra | α-2,6 sialic acid on LacNAc | Sialic, Lac |
| SSA | Salvia sclarea lectin | Terminal GalNAc linked to serine | GalNAc |
| STL | Solanum tuberosum | (GlcNAc)3, LacNAc | GlcNAc |
| UEA-I | Ulex Europaea Aggl | α-1,3-Fuc. L-fucose | Fuc |
| VFA | Vicia faba lectin | α-Man, Glc, GlcNAc | Mannose |
| VVL | Vicia villosa B4 | GalNAc | GalNAc |
| WFL | Wisteria floribunda | GalNAc | GalNAc |
| WGA | Triticum Vulgaris | (GlcNAc)n, sialic acid | GlcNAc |
Table listing the 48 lectins we print in our default setup
Custom Lectin microarrays:
Asparia also offers custom lectin microarrays featuring C-type lectins and Siglecs, as part of its Human Immune Lectin Assay platform.
How we work for the lectin microarray service
Our workflow ensures a clear, straightforward, and transparent process for sample glycoanalysis
Sample
Let us know which type of sample (purified protein, antibodies, cells, tissue, etc.) you want to analyze, and our team will evaluate the feasibility.
Sample labeling
We use a fluorescent dye and sample cleanup.
Optimization
We optimize the sample concentration and incubation conditions on the test slide.
Lectin binding analysis
Generally, in triplicate (4 samples/slide), but let us know your needs to accommodate the samples.
Microarray Quantification
The latest technology – A Scienion S11 microarray spotter and an Agilent G2565BA microarray scanner – are used
Data processing
Our experts analyze and interpret the data to transform it into actionable information.
Report
A publication-type report that includes the Materials & Methods, with data interpretation easy to visualize in histograms. We also provide the raw data.
Purposes and applications for lectin microarray
Lectin microarray of a purified glycoprotein or more complex biological matrices serves several purposes and applications:
Oncology
Lectin microarrays are widely used to identify aberrant glycosylation patterns in tumor cells or serum glycoproteins. Tumors often exhibit changes in glycan structures—such as increased sialylation or fucosylation—which can be detected sensitively with lectin arrays. This helps in biomarker discovery, patient stratification, and monitoring treatment responses
Infectious Disease
Because glycan patterns often shift earlier than protein levels, lectin arrays are powerful tools to provide sensitive, non-invasive diagnostic options and companion tests for conditions like cancer, autoimmune diseases, or infections
Immune and Inflammatory Diseases
As glycosylation can regulate immune cell communication, antibody function, and inflammation, detecting specific bindings to glycan patterns on cytokines, antibodies, or receptors provides insight into immune regulation and guides the development of immunotherapies
Microbiome
Lectin microarrays can help examine glycan-mediated interactions between host and microbes, since they allow for profiling glycoproteins in the gut mucosa or microbial secretions
Biomarkers & diagnostics
Lectin arrays enable high-throughput profiling of glycan patterns on biomolecules, facilitate the discovery of glycosylation-based biomarkers for disease, and their sensitivity and specificity support early diagnosis and patient stratification
Other Fields
- Plant science: used to study cell wall glycoproteins and stress-related glycosylation changes.
- Agriculture: evaluating glycoprotein content in crops or engineered plants
- Nutraceuticals and Cosmetics: support quality control of bioactive glycoproteins, ensuring consistent glycan profiles. In the Human Milk Oligosaccharides (HMOs) field, lectin arrays help characterize glycan patterns relevant to infant gut health and immune development
Related publications
A selection of our most relevant scientific publications related to our lectin microarray service
Williams C, Royo F, Aizpurua-Olaizola O, Pazos R, Boons G-J, Reichardt N-C, et al. Glycosylation of extracellular vesicles: current knowledge, tools and clinical perspectives. J Extracell Vesicles. 2018;7(1):1442985
Pazos R, Echevarria J, Hernandez A, Reichardt N-C. Lectin-array blotting. Curr Protoc Cell Biol. 2017;76(1):6.12.1-6.12.12.
Brzezicka K, Vogel U, Serna S, Johannssen T, Lepenies B, Reichardt N-C. Influence of core β-1,2-xylosylation on glycoprotein recognition by Murine C-type lectin receptors and its impact on dendritic cell targeting. ACS Chem Biol. 2016;11(8):2347–56.
Etxebarria J, Calvo J, Martin-Lomas M, Reichardt N-C. Lectin-array blotting: profiling protein glycosylation in complex mixtures. ACS Chem Biol. 2012;7(10):1729–37.
Echevarria J, Royo F, Pazos R, Salazar L, Falcon-Perez JM, Reichardt N-C. Microarray-based identification of lectins for the purification of human urinary extracellular vesicles directly from urine samples. Chembiochem. 2014;15(11):1621–6.
