The present disclosure relates to the characterization and production of biologics.

Disclosed are an antibody or a functional fragment thereof binding to 3′-sialyl lactose and comprising a heavy chain variable region which is optionally substituted with 3 or less amino acids and which comprises a CDR sequence consisting of an amino acid sequence ARKNGGLDYAMDY (SEQ ID NO: 3), a polynucleotide encoding the antibody or the functional fragment thereof, an expression vector comprising the polynucleotide, and a test drug for a disease and a pharmaceutical composition comprising the antibody or the functional fragment thereof.

There is provided compositions for the detection of target cellular material, the composition comprising: a chemically modified substrate; at least one binding moiety, wherein the binding moiety comprises a glycan; and at least one linker covalently linked to the substrate and the binding moiety by a first and second bond. There is also provided methods of preparation of such compositions and methods for detection of target cellular material, such as for detection of pathogenic microorganisms.

The present disclosure relates to the characterization and production of biologics.

Antibody molecules that specifically bind to APRIL are disclosed. The antibody molecules can be used to treat, prevent, and/or diagnose disorders, such as IgA nephropathy.

The present invention provides glycated Amadori products of the CD59 peptide and fragments thereof to be used as tools and among methods for the diagnosis and prognosis of pre-diabetes and diabetes. Certain aspects of the invention include glycated Amadori products of CD59 and fragments thereof to be used for the generation of antibodies and antibody fragments. Still other aspects of the invention include methodologies for the preparation of glycated Amadori products of CD59, fragments thereof, the inventive antibodies, and antibody fragments.

Provided is at least one method of suppressing, in an immunoassay using surface plasmon-field enhanced fluorescence spectroscopy (SPFS), nonspecific signals generated by nonspecific adsorption of contaminants contained in a sample to an SPFS sensor section (e.g., a primary antibody, a solid-phase layer and a metal thin film). At least one method relates to a method of suppressing nonspecific signals originating from contaminants in an immunoassay using surface plasmon-field enhanced fluorescence spectroscopy (SPFS) (including cases where a receptor for a compound to be measured is used in place of a primary antibody), the method comprising performing at least one pretreatment.

Embodiments described herein generally relate to technologies for analyzing peptide structures for diagnosing and/or treating a disease state advancing through a disease progression. A non-limiting example of a method relating to the technologies described in the subject application may include receiving peptide structure data corresponding to the biological sample obtained from the subject, identifying a peptide structure profile, and diagnosing a disease state within a disease progression. The example may further include generating a diagnosis output relating to the disease state. In at least some cases, the peptide structure profile may include glycosylated peptides, aglycosylated peptides, or both.

Methods are provided for making rapid labeled dextran ladders and other calibrants useful in liquid chromatography. The methodologies include a two-step process comprising a reductive amination step of providing a reducing glycan and reacting it with a compound having a primary amine to produce an intermediate compound. The intermediate compound is then rapidly tagged with a rapid tagging reagent to produce the rapid labeled dextran ladder.

Methods for peptide and/or protein quantification by mass spectrometry using labeled peptides, wherein multiple labels lead to distinct fragments for the labeled peptides and their unlabeled variant, thus facilitating data analysis and enhancing the potential for quantification. Methods for selecting the label and label position are further given, as well as sets of labeled peptides resulting from or for use in the above-mentioned methods. The methods and substances are especially useful for data-independent or multiplexed parallel reaction monitoring proteomics applications involving peptide quantification.