Abstract: Systems and methods to characterize dimerization interfaces at the subdomain level of a protein are provided. An exemplary method includes digesting a protein dimer sample into subdomains, labeling the digested protein sample, isolating labeled dimeric and monomeric subdomain fragments, and peptide mapping the labeled sample to determine where the dimer fragments are labeled and where the dimer fragments are not labeled. Regions that show decreased labeling extents in the dimer fraction than that in the monomer fraction are likely involved or in close proximity to the dimerization interface.

Abstract: The present invention provides rapid, sensitive high-throughput methods and systems for characterizing peptides or proteins using hydrophobic interaction chromatography-coupled native mass spectrometry to improve manufacturing process of biopharmaceutical products, such as identifying impurities during antibody purification, monitoring post-translational modification variants during production, or characterizing drug-to-antibody ratio of antibody-drug conjugates. The separation profiles of the peptides or proteins are generated and compared to identify or qualify the peptides or proteins.

Abstract: Methods and system for identifying and quantifying antibody fragments and identifying the site of fragmentation on an antibody are provided herein.

Abstract: The present inventions provide new and improved systems and methods combining asymmetrical flow field-flow fractionation (A4F, and also referred to as AF4) and mass spectrometry (MS) in order to analyze for biomacromolecules, including but not limited to Fc-antibodies, antibody fragments, fusion proteins, Fc-fusion proteins, receptor Fc-fusion proteins, trap proteins and mini-trap proteins. Nanoparticles also can be analyzed.

Abstract: The present invention generally pertains to methods of characterizing of a protein of interest. In particular, the present invention pertains to the use of post-column denaturation, size exclusion chromatography and mass spectrometry for detecting, identifying and characterizing crosslinking amino acid residues in a therapeutic antibody.

Abstract: The present inventions generally pertains to methods of characterizing of a protein of interest. In particular, the present inventions pertains to the use of native immunoprecipitation and native strong cation exchange chromatography-mass spectrometry for identifying and quantifying the pairing products of two or more antibodies co-expressed in vivo.

Abstract: Methods and system for identification of dimer species using online chromatography and electrospray ionization mass spectrometry are provided. Also provided are methods and system for quantitation of heterodimer species using immunoprecipitation and liquid chromatography-mass spectrometry.

Abstract: Methods and system for identifying and quantifying antibody fragments and identifying the site of fragmentation on an antibody are provided herein.

Abstract: The present invention provides rapid, sensitive high-throughput methods and systems for characterizing peptides or proteins using hydrophobic interaction chromatography-coupled native mass spectrometry to improve manufacturing process of biopharmaceutical products, such as identifying impurities during antibody purification, monitoring post-translational modification variants during production, or characterizing drug-to-antibody ratio of antibody-drug conjugates. The separation profiles of the peptides or proteins are generated and compared to identify or qualify the peptides or proteins.

Abstract: Methods and system for identification of dimer species using online chromatography and electrospray ionization mass spectrometry are provided. Also provided are methods and system for quantitation of heterodimer species using immunoprecipitation and liquid chromatography-mass spectrometry.

Abstract: The present invention relates to the field of protein characterization, and in particular to methods for identifying critical quality attributes of therapeutic proteins by implementing a workflow including using a competitive binding assay with insufficient capture molecule followed by LC-MS.

Abstract: The present invention provides rapid, sensitive high-throughput methods and systems for characterizing peptides or proteins using hydrophobic interaction chromatography-coupled native mass spectrometry to improve manufacturing process of biopharmaceutical products, such as identifying impurities during antibody purification, monitoring post-translational modification variants during production, or characterizing drug-to-antibody ratio of antibody-drug conjugates. The separation profiles of the peptides or proteins are generated and compared to identify or qualify the peptides or proteins.

Abstract: The present invention relates to the field of protein characterization, and in particular to methods for identifying critical quality attributes of therapeutic proteins by implementing a workflow including using a competitive binding assay with insufficient capture molecule followed by LC-MS.

Abstract: The present invention generally pertains to methods of characterizing antibodies and related products. In particular, the present invention pertains to the use of immunoprecipitation and postcolumn denaturation-assisted native size exclusion chromatography-mass spectrometry to specifically and sensitively detected and quantitate antibodies and related products in a sample.

Abstract: Methods and system for identifying and quantifying antibody fragments and identifying the site of fragmentation on an antibody are provided herein.

Abstract: Methods and system for identifying and/or quantifying a protein are provided herein.

Abstract: Disclosed are native liquid chromatography-mass spectrometry systems and methods of use. A native liquid chromatography-mass spectrometry system can include a liquid chromatography system capable of separating a sample; and an electrospray ionization mass spectrometry (ESI-MS) system in fluid communication with the liquid chromatography system, wherein the ESI-MS system comprises a multi-nozzle electrospray ionization emitter and a system for modifying a desolvation gas and a mass spectrometer, wherein the mass spectrometer is configured to receive ions and characterize mass to charge ratio of ions.

Abstract: The present invention provides rapid, sensitive high-throughput methods and systems for characterizing peptides or proteins using hydrophobic interaction chromatography-coupled native mass spectrometry to improve manufacturing process of biopharmaceutical products, such as identifying impurities during antibody purification, monitoring post-translational modification variants during production, or characterizing drug-to-antibody ratio of antibody-drug conjugates. The separation profiles of the peptides or proteins are generated and compared to identify or qualify the peptides or proteins.

Abstract: Methods and system for identifying and/or quantifying a protein are provided herein.

Abstract: Systems and methods to characterize dimerization interfaces at the subdomain level of a protein are provided. An exemplary method includes digesting a protein dimer sample into subdomains, labeling the digested protein sample, isolating labeled dimeric and monomeric subdomain fragments, and peptide mapping the labeled sample to determine where the dimer fragments are labeled and where the dimer fragments are not labeled. Regions that show decreased labeling extents in the dimer fraction than that in the monomer fraction are likely involved or in close proximity to the dimerization interface.