Systems and methods for characterizing low molecular weight (LMW) protein drug product impurities are provided. One embodiment uses hydrophilic interaction chromatography (HILIC) coupled to mass spectrometry analysis. After removal of the N-linked glycans from the protein drug product, for example an antibody drug product, the elution of LMW impurities from the HILIC column was determined by the size of the molecular weight species. In some embodiments, the HILIC separation is performed under denaturing conditions, making the detection of LMW forms using this method highly comparable to both SDS-PAGE and CE-SDS methods. LMW drug product impurities include, but are not limited to light chain, half antibody, H2L, H2, HL, HC, peptide backbone-truncated species, and combinations thereof.

Disclosed is a polypeptide including a mutated Fc region and having functional activity, mediated by the Fc region, that is modified compared with that of a parent polypeptide. The Fc region includes at least one combination of 2 mutations, the combination being selected from among one mutation selected from among a first set of mutations, and at least one mutation selected from among a second set of mutations, and provided that mutation (i) does not take place on the same amino acid as mutation (ii). Also disclosed are use of the polypeptide, compositions including the same, and methods for preparing the polypeptide.

A method of ionising a sample is disclosed comprising nebulising a sample which includes first biomolecules such as bovine insulin comprising one or more disulphide (S—S) bonds. A stream of droplet or charged droplets comprising one or more disulphide (S—S) bonds is directed so as to impact upon a target (106) or electrode so as to cause the breaking of a portion of the disulphide bonds. Alternatively, charged droplets may pass through an electric field region determined by an electrode (106) arranged downstream of a nebuliser or electrospray probe and an ion inlet (104) of a mass spectrometer so as to cause the breaking of a portion of the disulphide bonds.

Provided herein are compositions, kits, and methods for performing analyte detection immunoassays.

Herein is reported a method for selecting an antibody with a systematic clearance in cynomolgus monkeys of less than 8 mL/kg/day comprising the steps of measuring the retention time of the antibody on performing an FcRn affinity chromatography with a positive linear pH gradient and on a heparin affinity chromatography with a positive linear conductivity/salt gradient, and selecting an antibody that has a relative retention time on the FcRn affinity chromatography column is less than 1.78 times the retention time difference between peaks 2 and 3 the retention time of preparation of an oxidized anti-Her3 antibody of SEQ ID NO: 03 and 04, and a relative retention time on the heparin affinity chromatography column is less than 0.87 times the retention time of an anti-pTau antibody of SEQ ID NO: 01 and 02.

Disclosed is a method of diagnosing multiple sclerosis (MS), wherein a blood sample from a patient is incubated with a DNA-replication associated (REP) protein. The present invention relates to a DNA-replication-associated (Rep) protein for use in the diagnosis of multiple sclerosis (MS), wherein (a) an increased amount of Rep protein or fragments thereof in the sample as compared to an amount in a control sample; or an increased amount of anti-Rep protein antibodies with antigen in a sample from a subject as compared to an amount in a control sample correlates with a diagnosis of MS, wherein the Rep protein is MSBI1 Rep or MSBI2 Rep.

The present invention provides an antibody including a structural domain represented by the following amino acid sequence, in an N- to C-direction, N-FR1-CDR1-FR2-CDR2-FR3-CDR3-FR4-C
wherein the antibody further includes a protein molecule bound to the structural domain; the structural domain is capable of binding to a norovirus; FR denotes a framework region amino acid sequence and CDR denotes a complementary determining region amino acid sequence; any one of the following requirements (i)-(iii) is satisfied. Requirement (i): the CDR1 includes an amino acid sequence having a sequence identity of not less than 60% with any one of the amino acid sequences represented by SEQ ID NO: 1-SEQ ID NO: 6, the CDR2 includes an amino acid sequence having a sequence identity of not less than 60% with any one of the amino acid sequences represented by SEQ ID NO: 7-SEQ ID NO: 12, and the CDR3 includes an amino acid sequence having a sequence identity of not less than 60% with any one of the amino acid sequences represented by SEQ ID NO: 13-SEQ ID NO: 17; Requirement (ii): the CDR1 includes an amino acid sequence in which one-three amino acid(s) of any one of the amino acid sequence represented by SEQ ID NO: 1-SEQ ID NO: 6 has/have been substituted, deleted, or added, the CDR2 includes an amino acid sequence in which one-three amino acid(s) of any one of the amino acid sequence represented by SEQ ID NO: 7-SEQ ID NO: 12 has/have been substituted, deleted, or added, and the CDR3 includes an amino acid sequence in which one-three amino acid(s) of any one of the amino acid sequence represented by SEQ ID NO: 13-SEQ ID NO: 17 has/have been substituted, deleted, or added; and Requirement (iii): the CDR1 includes any one of the amino acid sequence represented by SEQ ID NO: 1-SEQ ID NO: 6, the CDR2 includes any one of the amino acid sequence represented by SEQ ID NO: 7-SEQ ID NO: 13, and the CDR3 includes any one of the amino acid sequence represented by SEQ ID NO: 13-SEQ ID NO: 17.

This invention provides, and in certain specific but non-limiting aspects relates to: assays that can be used to predict whether a given ISV will be subject to protein interference as described herein and/or give rise to an (aspecific) signal in such an assay (such as for example in an ADA immunoassay). Such predictive assays could for example be used to test whether a given ISV could have a tendency to give rise to such protein interference and/or such a signal; to select ISV's that are not or less prone to such protein interference or to giving such a signal; as an assay or test that can be used to test whether certain modification(s) to an ISV will (fully or partially) reduce its tendency to give rise to such interference or such a signal; and/or as an assay or test that can be used to guide modification or improvement of an ISV so as to reduce its tendency to give rise to such protein interference or signal; —methods for modifying and/or improving ISV's to as to remove or reduce their tendency to give rise to such protein interference or such a signal; —modifications that can be introduced into an ISV that remove or reduce its tendency to give rise to such protein interference or such a signal; ISV's that have been specifically selected (for example, using the assay(s) described herein) to have no or low(er)/reduced tendency to give rise to such protein interference or such a signal; modified and/or improved ISV's that have no or a low(er)/reduced tendency to give rise to such protein interference or such a signal.

This document relates to methods for detecting and quantifying heavy and light chains of immunoglobulin using mass spectrometry techniques.

This invention provides, and in certain specific but non-limiting aspects relates to: assays that can be used to predict whether a given ISV will be subject to protein interference as described herein and/or give rise to an (aspecific) signal in such an assay (such as for example in an ADA immunoassay). Such predictive assays could for example be used to test whether a given ISV could have a tendency to give rise to such protein interference and/or such a signal; to select ISV's that are not or less prone to such protein interference or to giving such a signal; as an assay or test that can be used to test whether certain modification(s) to an ISV will (fully or partially) reduce its tendency to give rise to such interference or such a signal; and/or as an assay or test that can be used to guide modification or improvement of an ISV so as to reduce its tendency to give rise to such protein interference or signal; methods for modifying and/or improving ISV's to as to remove or reduce their tendency to give rise to such protein interference or such a signal; modifications that can be introduced into an ISV that remove or reduce its tendency to give rise to such protein interference or such a signal; ISV's that have been specifically selected (for example, using the assay(s) described herein) to have no or low(er)/reduced tendency to give rise to such protein interference or such a signal; modified and/or improved ISV's that have no or a low(er)/reduced tendency to give rise to such protein interference or such a signal.