Abstract: This disclosure relates to antibody-drug conjugates (ADCs) comprising an anti-Trop-2 antibody. Provided herein are compositions comprising such ADCs, as well as methods of making and using the same.

Abstract: Provided herein are anti-LAP antibodies (e.g., recombinant humanized, chimeric, and human anti-LAP antibodies) or antigen binding fragments thereof which have therapeutically beneficial properties, such as binding specifically to LAP-TGF?1 on cells but not to LAP-TGF?1 in extracellular matrix, as well as compositions including the same. Also provided are uses of these antibodies or antigen binding fragments in therapeutic applications, such as in the treatment of cancer, and diagnostic applications.

Abstract: Provided herein are anti-LAP antibodies (e.g., recombinant humanized, chimeric, and human anti-LAP antibodies) or antigen binding fragments thereof which have therapeutically beneficial properties, such as binding specifically to LAP-TGF?1 on cells but not to LAP-TGF?1 in extracellular matrix, as well as compositions including the same. Also provided are uses of these antibodies or antigen binding fragments in therapeutic applications, such as in the treatment of cancer, and diagnostic applications.

Abstract: This invention relates to the treatment of chronic kidney disease, including diabetic nephropathy, focal segmental glomerulosclerosis (FSGS), nephrotic syndrome, non-diabetic chronic kidney disease, renal fibrosis or acute kidney injury by the administration of an RGD mimetic integrin receptor antagonist, either as a single agent or in combination with other agents.

Abstract: This invention relates to the treatment of chronic kidney disease, including diabetic nephropathy, focal segmental glomerulosclerosis (FSGS), nephrotic syndrome, non-diabetic chronic kidney disease, renal fibrosis or acute kidney injury by the administration of an RGD mimetic integrin receptor antagonist, either as a single agent or in combination with other agents.

Abstract: The present invention relates generally to novel protein modification reagents for fractionation and quantitative (differential) profiling of proteins in a complex mixture. The reagents react with amino acids or other protein components or structures and function as mass tags. The present invention provides methods of making the protein modification reagents and methods of using the protein modification reagents for quantitative analysis of proteins.

Abstract: Relative quantitative information about components of chemical or biological samples can be obtained from mass spectra by normalizing the spectra to yield peak intensity values that accurately reflect concentrations of the responsible species. A normalization factor is computed from peak intensities of those inherent components whose concentration remains constant across a series of samples. Relative concentrations of a component occurring in different samples can be estimated from the normalized peak intensities. Unlike conventional methods, internal standards or additional reagents are not required. The methods are particularly useful for differential phenotyping in proteomics and metabolomics research, in which molecules varying in concentration across samples are identified. These identified species may serve as biological markers for disease or response to therapy.

Abstract: The present invention relates generally to novel protein modification reagents for fractionation and quantitative (differential) profiling of proteins in a complex mixture. The reagents react with amino acids or other protein components or structures and function as mass tags. The present invention provides methods of making the protein modification reagents and methods of using the protein modification reagents for quantitative analysis of proteins.

Abstract: Relative quantitative information about components of chemical or biological samples can be obtained from mass spectra by normalizing the spectra to yield peak intensity values that accurately reflect concentrations of the responsible species. A normalization factor is computed from peak intensities of those inherent components whose concentration remains constant across a series of samples. Relative concentrations of a component occurring in different samples can be estimated from the normalized peak intensities. Unlike conventional methods, internal standards or additional reagents are not required. The methods are particularly useful for differential phenotyping in proteomics and metabolomics research, in which molecules varying in concentration across samples are identified. These identified species may serve as biological markers for disease or response to therapy.

Abstract: The present invention relates generally to novel protein modification reagents for fractionation and quantitative (differential) profiling of proteins in a complex mixture. The reagents react with amino acids or other protein components or structures and function as mass tags. The present invention provides methods of making the protein modification reagents and methods of using the protein modification reagents for quantitative analysis of proteins.

Abstract: A method of separating a mixture of biopolymers of various lengths using a blend of two linear hydrophilic polymers, particularly polyacrylamides (LPA) or substituted polyacrylamides, one with high weight-average molecular mass and another with low weight-average molecular mass, each present at a low concentration but wherein the concentration of the high weight-average molecular mass LPA is above its entanglement threshold, is disclosed. The matrix is excellent for use in methods of nucleic acid analysis, particularly long read length DNA sequencing.

Abstract: A liquid chromatography-electrospray ionization mass spectrometry method is capable of separating and identifying different prostaglandin isomers, including PGD2 and PGE2. Unlike traditional gas chromatography methods, little sample preparation and no derivatization are required. The chromatography is performed under acidic conditions that are optimal for separating the isomers. A basic sheath flow liquid is added to the chromatographic eluent, resulting in high ionization efficiency when the electrospray ionization is performed in negative ion mode. Additionally, by altering the energy at which the ionization is performed, tandem mass spectra of the two isomers can be made to differ as a result of the different relative energies of the two isomers.