Provided are a recombinant N protein of SARS-CoV-2 and methods for preparing the same and for purifying the same. The recombinant N protein of SARS-CoV-2 has an N protein sequence, wherein each of both ends of the N protein sequence are linked to an oligolysine fragment. An expression method for the recombinant N protein includes: a. providing a sample including the recombinant N protein; and b. performing cation exchange chromatography resin purification treatment at least once, and collecting breakthrough substance. The method may effectively improve the expression purity of the recombinant N protein.

The present invention comprises conjugates comprising a monoclonal antibody conjugated to a cyclic PYY peptide. The invention also relates to pharmaceutical compositions and methods for use thereof. The novel conjugates are useful for preventing, treating or ameliorating diseases and disorders disclosed herein.

The present invention comprises conjugates comprising a monoclonal antibody conjugated to a cyclic PYY peptide. The invention also relates to pharmaceutical compositions and methods for use thereof. The novel conjugates are useful for preventing, treating or ameliorating diseases and disorders disclosed herein.

The present invention discloses a preparation method for a disubstituted PEGylated interleukin 2, which comprises the steps of: (1) PEGylating IL-2 to obtain a crude product of a PEGylated interleukin; (2) performing gel chromatography filtration to remove free interleukin 2 from the crude product; (3) performing affinity chromatography on the product in the step (2) by means of an α receptor column, and collecting a flow-through peak component and an elution peak component; (4) performing ion exchange separation on the flow-through peak component and the elution peak component in the step (3); and (5) collecting components of the disubstituted PEGylated interleukin 2.

The present invention discloses a preparation method for a disubstituted PEGylated interleukin 2, which comprises the steps of: (1) PEGylating IL-2 to obtain a crude product of a PEGylated interleukin; (2) performing gel chromatography filtration to remove free interleukin 2 from the crude product; (3) performing affinity chromatography on the product in the step (2) by means of an α receptor column, and collecting a flow-through peak component and an elution peak component; (4) performing ion exchange separation on the flow-through peak component and the elution peak component in the step (3); and (5) collecting components of the disubstituted PEGylated interleukin 2.

The present invention relates to a process for purifying C1-esterase inhibitor (C1-Inh), and more in particular a Cl-Inh concentrate.

The present invention relates to a process for purifying C1-esterase inhibitor (C1-Inh), and more in particular a Cl-Inh concentrate.

A method for purification of a sulfatase using metal chelating chromatography without using tags such as His-tag, etc. is disclosed. An embodiment provides a method for purifying a sulfatase including the steps of: (a) providing a sulfatase-containing solution comprising one or a plurality of impurities; (b) performing a first chromatographic separation of the sulfatase-containing solution using a metal affinity chromatography resin; (c) performing a second chromatographic separation using a cation exchange chromatography resin; and (d) performing a final chromatographic separation using an anion exchange chromatography resin, wherein the impurities are removed thereby.

A method for purification of a sulfatase using metal chelating chromatography without using tags such as His-tag, etc. is disclosed. An embodiment provides a method for purifying a sulfatase including the steps of: (a) providing a sulfatase-containing solution comprising one or a plurality of impurities; (b) performing a first chromatographic separation of the sulfatase-containing solution using a metal affinity chromatography resin; (c) performing a second chromatographic separation using a cation exchange chromatography resin; and (d) performing a final chromatographic separation using an anion exchange chromatography resin, wherein the impurities are removed thereby.

The present invention is in the field of purification and protein purification in particular. The invention provides improved techniques for the industrial-scale purification of proteins and other biomolecules. More specifically, it relates to a process for the purification of a compound of interest, such as a protein, preferably an antibody or an antibody fragment using a chromatography step, preferably a semi-continuous chromatography step.