Matrix assisted laser desorption ionization (MALDI) is a very popular ionization process widely used for proteins and peptides characterization. The presented technology enables modification of almost any conductive material including indium-tin oxide (ITO) glass, aluminum, stainless steel or conductive polymers. The MALDI targets are functionalized by reactive landing of ions under atmospheric conditions. The MALDI plates can be modified by proteins, peptides or by inorganic compounds such titanium dioxide or zirconium dioxide. Proteins, such as enzymes, lectins or antibodies stick after the deposition on the surface very efficiently and remain active. The activity is used for "on plate" digestion or enrichment of different types of antigens or compounds.
MALDI targets with immobilized proteases used for rapid in-situ digestion of proteins. You can select from the following proteases and design your own chip. The MALDI targets are prepared with different geometry and number of spots up to 80 positions.
- Pepsin, Nepenthesin-1, Nepenthesin-2, Rhizopuspepsin, Aspergillopepsin, Trypsin, Subtilisin, Chymotrypsin, Customized
MALDI targets immobilized with different type of lectins for in-situ enrichment of glycans and glycopeptides. We currently offer following lectin chips
- WGA (wheat germ agglutinin), Con A (Concanavalin A), Customized
MALDI targets with immobilized antibodies or other affinity proteins for enrichment of antigens from different types of matrices.MALDI targets immobilized with different type of lectins for in-situ enrichment of glycans and glycopeptides.
- antibodies, biotin-binding proteins (avidin, streptavidin, neutravidin)
A new mass spectrometry-based approach for determination of haptoglobin phenotype from human serum samples. The simple workflow utilizes in-situ immunoaffinity enrichment on antibody functionalized MALDI plates. The MALDI mass spectra of haptoglobin alpha chains enriched on the MALDI plates by specific interaction with the anti-haptoglobin antibody show ion signals of alpha subunits at m/z 9192 and at m/z 15945, which allows immediate and straightforward determination of the haptoglobin phenotype (Pompach P. et al., Clinical Chemistry 2016).
Carbohydrate Deficient Transferrin (CDT)
Transferrin is synthetized in the liver and is the most important iron-transport carrier in the human body. Severe alcohol consumption leads to alterations in glycosylation of transferrin (CDT). Mass spectrometry can provide fast detection and quantification of transferrin isoforms since they have different molecular masses. Antibody chips prepared by ambient soft ion landing in combination with MALDI -TOF are used for detection and quantification of transferrin isoforms.