The invention describes an efficient platform for antibody manufacturing and formulation that provides i) cell culture process with improved feeding strategy resulting in high antibody titer between 2 gm/L to 5 gm/L; ii) improved purification process showing optimal percentage recovery, high purity monomer content, minimum aggregation/particulate formation, minimum impurity levels; and iii) high concentration stable liquid formulation with optimal osmolality and low viscosity across different temperature excursions and devoid of aggregation. The preferred antibodies include IgG1 monoclonal antibody specific to the Dengue virus epitope in domain III of the E protein and IgG1 monoclonal antibody specific to the rabies virus surface G glycoprotein.

Disclosed herein are methods for purifying a recombinant protein from a composition comprising the recombinant protein and at least one impurity, the methods comprising performing anion exchange chromatography (e.g., in flow-through or weak partitioning chromatography mode) using an anion exchange material comprising a primary amine ligand, such as a polyamine ligand.

Provided is a cyclic peptide, which is represented by Formula (I) or Formula (I) and has excellent antibody binding properties and improved chemical resistance, an affinity chromatography support, a labeled antibody, an antibody drug conjugate, and a pharmaceutical preparation.

R.sup.N-X.sub.g-[X.sub.i-X.sup.a-X.sub.m-X.sup.2-X.sup.3-X.sub.n-X.sup.b-X.sub.j].sub.k-X.sub.h-R.sup.C(I)

In Formula (I), X.sup.a and X.sup.b each independently represent an amino acid residue derived from an amino acid, other than L-cysteine and D-cysteine, having a thiol group on a side chain and are bonded to each other through a disulfide bond, or, one of X.sup.a and X.sup.b represents an amino acid residue derived from an amino acid, other than L-cysteine and D-cysteine, having a thiol group on a side chain and the other represents an amino acid residue derived from an amino acid having a haloacetyl group on a side chain, and X.sup.a and X.sup.b are bonded to each other through a thioether bond.

R.sup.N-X.sub.g-[X.sub.i-X.sup.a-X.sub.m-X.sup.1-X.sup.2-X.sup.3-X.sub.n-X.sup.b-X.sub.j].sub.k-X.sup.h-R.sup.C(I)

In Formula (I), one of X.sup.a and X.sup.b represents an amino acid residue derived from L-cysteine or D-cysteine and the other represents an amino acid residue derived from an amino acid having a haloacetyl group on a side chain, and X.sup.a and X.sup.b are bonded to each other through a thioether bond, or, one of X.sup.a and X.sup.b represents an amino acid residue derived from L-penicillamine or D-penicillamine and the other represents an amino acid residue derived from an amino acid having a haloacetyl group on a side chain, and X.sup.a and X.sup.b are bonded to each other through a thioether bond.

Disclosed herein are methods for the isolation and purification of anti-IL-13 antibodies wherein the use of an affinity chromatographic step results in an antibody composition sufficiently pure for pharmaceutical uses. The methods described herein comprise pH viral reduction/inactivation, ultrafiltration/diafiltration, affinity chromatography (e.g., Protein A affinity chromatography), ion exchange chromatography, and hydrophobic chromatography. Further, the present invention is directed toward pharmaceutical compositions comprising one or more antibodies of the present invention.

The present invention relates to a preparation method of a human plasma-derived hepatitis B immunoglobulin preparation. More specifically, the present invention relates to a preparation method of a human plasma-derived hepatitis B immunoglobulin preparation characterized in that plasma protein fraction II (fraction II) containing human hepatitis B immunoglobulin is dialysis concentrated and then thrombus-producing materials and impurities formed during processes are removed by anion exchange resin and cation exchange resin purification techniques. By using the preparation method of the human plasma-derived hepatitis B immunoglobulin preparation according to the present invention, the efficiency of removing impurities and thrombus-producing materials is increased and a polymer content is maintained, whereby it is possible to produce human hepatitis B immunoglobulin with stable and improved quality.

Disclosed herein are methods for the isolation and purification of anti-IL-13 antibodies wherein the use of an affinity chromatographic step results in an antibody composition sufficiently pure for pharmaceutical uses. The methods described herein comprise pH viral reduction/inactivation, ultrafiltration/diafiltration, affinity chromatography (e.g., Protein A affinity chromatography), ion exchange chromatography, and hydrophobic chromatography. Further, the present invention is directed toward pharmaceutical compositions comprising one or more antibodies of the present invention.

The invention provides a conjugate with fluorochrome moiety F coupled to a targeting moiety T. Moiety F is described by formula (I), and the targeting moiety T is characterised in that it has affinity to a tumour marker, such as an antibody or antibody fragment. The conjugate may be used for tumour diagnostics including photodetection of tumour nodules during resection surgery.

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.

Methods for viral clearance using low pH hold based on a statistical design of experiment are provided. Several factors are evaluated to characterize the impacts of a low pH hold step for virus inactivation, including the factors of pH conditions, conductivity conditions, protein type, temperature, acid titrant, spike timing, and post-spike filtration. In addition to the effect of pH on virus inactivation, an increase in ionic strength through manipulating the conductivity can be a key component that influences virus inactivation kinetics.

Herein is reported a method for producing or purifying an antibody using a mixed mode chromatography material that comprises ion exchange functional groups and hydrophobic interaction functional groups (MM HIC/TEX) operated in flowthrough mode, wherein the antibody is a hydrophilic antibody, and the antibody is applied in a solution comprising the antibody and an antichaotropic salt to the MM HIC/IEX chromatography material.