Aluminum coated glass slides provide a novel glycan array platform. Specifically, aluminum coated glass slides increase sensitivity of fluorescent based assay methods. Additionally, aluminum coated glass slides allows for mass spectroscopic analysis of carbohydrates and provide a platform for examining activity of cellulases. The unique properties of ACG slides include: the metal oxide layer on the surface can be activated for grafting organic compounds such as modified oligosaccharides; the surface remains electrically conductive, and the grafted oligosaccharides can be simultaneously characterized by mass spectrometry and carbohydrate-binding assay; and the slides are more sensitive than transparent glass slides in binding analysis.

The invention provides methods of treating -galactosidase A deficiency. Dosage forms, methods of administration, and methods of analyzing human -galactosidase A are also included.

Methods for determining glycation on a molecule and/or a glycan structure on a glycosylated molecule through the use of a combination of spectroscopic analysis and chemometric modeling are described. In addition, methods and systems for producing a molecule with a desired level of glycation, including a non-glycated molecule, and/or a desired level of a glycan structure on a glycosylated molecule are described.

Provided herein are methods for assessing cell surface glycans, e.g., N-glycans, by assessing a sample of released surface glycans, and determining the presence, absence, or level of glycans present in the sample. Also provided are methods of assaying and/or evaluating a cell composition by assessing the cell surface glycan profile of the cell composition and comparing the profile to a reference sample. Methods for manufacturing and/or culturing a plurality of cell compositions having consistent surface glycan expression with low variability are also provided.

The present invention relates to a kit for quantitative analysis of glycated hemoglobin (HbA1c), and the kit for quantitative analysis of HbA1c according to the present invention has excellent long-term stability of an enzyme reagent and thus has an effect of easily overcoming the disadvantages of the conventional reagents used in enzyme assays (e.g., storage, accuracy, portability, convenience of use, etc.).

Methods for derivatization of biomolecules including glycans or other biopolymers with one or more fluorescent, MS active compounds by reductive amination or rapid tagging in order to produce derivatized glycan having a pKa>7 and between about 200 and about 1000 of nonpolar surface area are described.

A test substrate for detecting a LAL-reactive substance, wherein at least a portion of said test substrate has been preloaded with at least one LAL reagent and/or at least one LAL-reactive standard. Methods of use of the test substrate are disclosed. Methods of depositing test reagents on a test substrate are also disclosed.

The present invention discloses a method of determining the presence of autoimmune disease with the use of glycan biomarkers. A method of improving the detection sensitivity of trace glycans from a mixture of glycans and a microfluidic chip therefor are also disclosed.

The presence of mild electrophiles, such as aldehydes, during the denaturation of glycoproteins or glycopeptides and subsequent enzymatic deglycosylation reduces artifacts in subsequent analyses of the glycans released from the glycoproteins or glycopeptides.

An integrated platform is provided for direct and unbiased label-free native analysis of N-glycans from single cells and biological samples as small as 1 nL or less. An in-capillary sample processing method is coupled with high-sensitivity label-free capillary electrophoresis and mass spectrometry. Direct, label-free characterization and quantification of single-cell surface N-glycomes can be performed with the detection of up to 100 N-glycans per single cell and up to 400 N-glycans per nL of blood. N-glycome alterations can be detected at the single-cell level for diagnosis of medical conditions. The platform also preserves cell integrity and therefore can be used for spatial glycomic and multiomic profiling at the single cell level.