Disclosed herein are reduced viscosity liquid formulations comprising a protein and an excipient compounds. Further disclosed are methods of reducing the viscosity of a liquid formulation comprising a protein, methods of treatment, and methods of improving protein processing.

The present invention provides a novel IGFR-like receptor and antagonists and agonists for targeting said receptor. Said antagonists and agonists are envisaged for use as a medicament, and in particular for treatment of diabetes.

The present invention generally pertains to methods of characterizing charge variants of a protein. In particular, the present invention pertains to the use of anion exchange chromatography-mass spectrometry (AEX-MS) methods using a salt-gradient. The present invention is particularly useful for charge variant analysis of IgG4 subclasses.

Provided herein are high affinity antibodies or antigen binding fragments thereof that specifically bind to human tau-pS413. Also provided are compositions, kits, methods, and uses involving such antibodies or antigen binding fragments thereof.

Provided herein, in some embodiments, are methods and compositions for purifying antibodies from cellular cultures using one or more thiol containing additives during a purification process, for example in a chromatographic purification process.

The present disclosure relates to a method of obtaining a cell where fucosylation pathways are modified, leading to production of partially fucosylated and non-fucosylated protein products, specifically antibodies from the cell. The present disclosure employs the Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR) technology. The method of the present disclosure targets the Fut8 gene and GMD gene in a cell. Such products are used in developing therapeutics and biomarkers, and in diagnosis and prognosis of diseases.

In various embodiments methods are provided for identifying a mammal having an elevated risk for an adverse cardiac event (e.g. an MI) and/or determining the prognosis for the mammal. In certain embodiments the methods comprise determining, or causing to be determined, the presence and/or level of antibodies that bind a malondialdehyde acetaldehyde adduct (MAA adduct) in a biological sample from the mammal, where an elevated level of anti-MAA adduct antibodies, as compared to the level found in a normal healthy mammal is an indicator that that said mammal has one or more atherosclerotic lesions and/or is at elevated risk for a myocardial infarction.

Biological small molecules, proteins or nucleic acids (target molecules, TM) are isolated in from biological media such as blood serum, cytoplasm, nucleoplasm etc. by a novel process (mate and separate) involving the use of PEGylated recognition molecule (PEG-RM) with high specificity and binding for TM, affording a macromolecular complex PEG-RM.TM, from which the target protein can be obtained in pure form.

The present disclosure discloses a method for expressing and preparing a bivalent bispecific antibody. In the present disclosure, each portion of a bivalent bispecific antibody and an immune hybrid protein thereof is respectively expressed in a suitable prokaryotic or eukaryotic cell system, separated and purified by high-performance affinity chromatography, and then spliced in vitro by trans-splicing reaction mediated by an intein, to prepare the bivalent specific antibody and an immune hybrid protein thereof.

The present invention relates to an improved method of purifying an immunoglobulin, and more particularly to a method of purifying an immunoglobulin which is capable of sufficiently removing impurities from an immunoglobulin-containing plasma protein sample through a simple process, comprising a single anion-exchange chromatography and a single cation-exchange chromatography.