Provided herein are formulations of PCSK9-binding polypeptides, such as those comprising evolocumab, that comprise N-acetyl arginine and have reduced viscosities when compared to formulations lacking N-acetyl arginine. Provided herein are also methods of formulating such compositions that are advantageous in that they conserve certain components. Such formulations comprising PCSK9-binding polypeptides can be administered to patients to treat and/or prevent PCSK9-related diseases, conditions, and disorders.

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.

The present invention relates to a purification process of recombinant antibody fragments from inclusion bodies expressed in microbial cells. More particularly, the present invention relates to a process for purification of recombinant humanized (rHu) antibody fragment, Ranibizumab from inclusion bodies expressed in microbial cells.

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.

Provided is a method of purifying a mixture of Fc-containing bioactive peptides by using an affinity column including an affinity matrix containing a protein A ligand, wherein the mixture of Fc-containing bioactive peptides includes a first Fc-containing bioactive peptide and a second Fc-containing bioactive peptide, and the second Fc-containing bioactive peptide includes at least one more human VH3 domain, compared to the first Fc-containing bioactive peptide. According to the purification method, bioactive peptides having the same or similar structures can be precisely separated to the high level of purity while simplification of the process is achieved.

The present invention relates to an improved method for peak fractionation and eluate collection during chromatography for purification of a human therapeutic antibody.

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.