The present invention pertains to an ophthalmic composition of Bevacizumab, in a single use prefilled syringe which is safe, non-toxic and efficacious for administration during the shelf life, characterised in that the ophthalmic solution is controlled with respect to the number of sub-visible particulate matter with significantly reduced endotoxin levels and with low aggregate level that are suitable for intravitreal use during the shelf life of 2 years of the product.

The present invention relates to a method for preparing a concentrate of polyvalent immunoglobulins with view to therapeutic use, from an initial solution of blood plasma or a plasma fraction enriched with immunoglobulins, comprising the steps for removing the protein contaminants by precipitation with caprylic acid in order to obtain a solution free of proteases, and for separating by chromatography on a fluidized bed the solution free of proteases, said method allowing a concentrate of human polyvalent immunoglobulins with a yield of more than 4.5 g of immunoglobulins per liter of blood plasma applied to be obtained.

Molecules, including antibodies and antigen-binding fragments thereof that specifically bind to a linker peptide, and methods of producing and using the described antibodies and antigen-binding fragments are presented herein. Also presented herein methods of generating antibodies that specifically bind to an immunorecessive epitope.

Disclosed are methods, compositions and uses of concentrated formulations of anti-CD74 antibody, of use for treating autoimmune diseases. In a specific non-limiting embodiment, the autoimmune disease is systemic lupus erythematosus (SLE). In a preferred embodiment, the anti-CD74 antibody is milatuzumab (IMMU-115). The antibody is administered subcutaneously, preferably at a dosage of 250 mg once a week for four weeks. The subcutaneous administration of anti-CD74 antibody ameliorates the symptoms of autoimmune diseases, with only manageable side effects.

There are provided efficient and cost-effective methods for purifying biomolecules in solution phase using stimuli-responsive protein-polymer conjugates. The protein-polymer conjugates comprise a target biomolecule-binding protein conjugated to a stimuli-responsive polymer and are reusable.

The present invention provides improved methods for the manufacturing of IVIG products. These methods offer various advantages such as reduced loss of IgG during purification and improved quality of final products. In other aspects, the present invention provides aqueous and pharmaceutical compositions suitable for intravenous, subcutaneous, and/or intramuscular administration. In yet other embodiments, the present invention provides methods of treating a disease or condition comprising administration of an IgG composition provided herein.

The present invention provides an improved manufacturing method for the production of bispecific antibody products, which comprise at least two binding domains. The process comprises at least the method comprising a step of refolding the construct, wherein one or more of the domains comprise a disulfide bond, and wherein the construct is contacted with a refolding buffer to refold the construct to its native form, the buffer comprising (i) a redox and/or oxidizing agent having a concentration of at least 0.1 mM and (ii) a chaotropic agent having a concentration >1 M, and wherein the pH of the refolding buffer corresponds to +/−4.5 of the pI value of the first domain or +/−4.0 of the pI value of the entire construct.

The invention provides methods for using and compositions of humanized antibodies that bind tau protein that is phosphorylated at the serine at position 413.

The present disclosure relates to methods of modifying the isoelectric point of an antibody. The method includes providing an antibody comprising a first polypeptide comprising a heavy chain variable region and a second polypeptide comprising heavy chain variable region and substituting, in at least one of the first and second polypeptides of the antibody, one or more amino acid residues of the heavy chain variable region (V.sub.H) at positions 7, 9, 11, 14, 41, 70, 74, 82a, 84, and 113, according to the Kabat numbering system, wherein the substituting increases or decreases the isoelectric point of the antibody.

The present invention relates method for purifying antibodies, said method comprising a limited number of steps while still allowing obtaining high yields of purified antibodies with an appropriate degree of purity. Briefly, this method comprises only filtration and precipitation steps, omitting the need for chromatography steps.