The present invention is broadly concerned with new in vitro glycosylation methods that provide rational approaches for producing glycosylated proteins, and the use of glycosylated proteins. In more detail, the present invention comprises methods of glycosylating a starting protein having an amino sidechain with a nucleophilic moiety, comprising the step of reacting the protein with a carbohydrate having an oxazoline moiety on the reducing end thereof, to covalently bond the amino sidechain of the starting protein with the oxazoline moiety, wherein the glycosylated protein substantially retains the structure and function of the starting protein. Target proteins include oxidase, oxidoreductase and dehydrogenase enzymes. The glycosylated proteins advantageously have molecular weights of at least about 7500 Daltons. In a further embodiment, the present invention concerns the use of glycosylated proteins, fabricated by the methods disclosed herein, in the assembly of amperometric biosensors.

The present invention is broadly concerned with new in vitro glycosylation methods that provide rational approaches for producing glycosylated proteins, and the use of glycosylated proteins. In more detail, the present invention comprises methods of glycosylating a starting protein having an amino sidechain with a nucleophilic moiety, comprising the step of reacting the protein with a carbohydrate having an oxazoline moiety on the reducing end thereof, to covalently bond the amino sidechain of the starting protein with the oxazoline moiety, wherein the glycosylated protein substantially retains the structure and function of the starting protein. Target proteins include oxidase, oxidoreductase and dehydrogenase enzymes. The glycosylated proteins advantageously have molecular weights of at least about 7500 Daltons. In a further embodiment, the present invention concerns the use of glycosylated proteins, fabricated by the methods disclosed herein, in the assembly of amperometric biosensors.

Disclosed is a method for producing an antibody, comprising culturing in a presence of a polyanionic compound an animal cell into which a gene encoding an antibody has been introduced whereby the animal cell produces the antibody, wherein the polyanionic compound is at least one selected from the group consisting of an anionic polysaccharide and an anionic polyamino acid, and the antibody is an antibody in which at least 3 amino acid residues of framework region 3 (FR3) are substituted each independently with an arginine residue or a lysine residue.

Disclosed is a method for producing an antibody, comprising culturing in a presence of a polyanionic compound an animal cell into which a gene encoding an antibody has been introduced whereby the animal cell produces the antibody, wherein the polyanionic compound is at least one selected from the group consisting of an anionic polysaccharide and an anionic polyamino acid, and the antibody is an antibody in which at least 3 amino acid residues of framework region 3 (FR3) are substituted each independently with an arginine residue or a lysine residue.

Disclosed in the present invention are an antibody targeting LAG-3, a preparation method therefor and the use thereof. In particular, disclosed in the present invention is a novel monoclonal antibody targeting LAG-3. Also disclosed in the present invention is a method for the preparation of the monoclonal antibody. The monoclonal antibody of the present invention is capable of binding LAG-3 antigens with high specificity, and has very high affinity and significant activities such as anti-tumor activity.

A method for cultivating a bacterial cell comprising the addition of an amino acid in an alkaline solution used for pH regulation. Also an aspect is a method for producing a polypeptide comprising the steps of a) providing a bacterial cell comprising a nucleic acid encoding the polypeptide, b) cultivating the provided cell, c) adjusting the pH value during the cultivating with a basic solution comprising an amino acid, d) recovering the polypeptide from the cell or the cultivation medium and thereby producing the polypeptide.

Provided herein are recombinant yeast cells having an active 3-Hydroxypropionic Acid (3-HP) pathway and further comprising a heterologous polynucleotide encoding an aspartate 1-decarboxylase (ADC) of the Class Insecta, Bivalvia, Branchioporia, Gastropoda, or Leptocardii. Also described are methods of using the recombinant yeast cells to produce 3-HP and acrylic acid.

A composition with an enhanced antifungal activity, which comprises peptides as a protamine hydrolysate and which is suitable for industrial application at a low cost, can be provided, by using a combination of a protamine hydrolysate and a terpene alcohol as an active ingredient of a composition having an antifungal activity.

The present invention relates to peptide manipulation systems and methods for modifying the folding trajectory and facilitating the folding of a polypeptide chain into native, non-native, or artificial conformations. The invention comprises applying movement restriction(s) and/or directional rotation(s) to a plurality of locations along a peptide backbone. The applied movement restriction(s) and/or directional rotation(s) are sufficient to achieve twisting or other conformation changes of different portions of the peptide backbone and thereby modify peptide folding trajectory and facilitate peptide folding.

The present invention relates to a top-down symmetric deconstruction approach which provides a novel alternative means to successfully identify a useful polypeptide “building block” for subsequent “bottom-up” de novo design of target protein architecture. The present invention also pertains to a novel peptides isolated by top-down symmetric deconstruction which may be useful for design or directed evolution of novel proteins with novel functionalities.