C07K1/16

CYSTEINE LINKED NANOBODY DIMERS

The present invention relates to dimers comprising a first polypeptide and a second polypeptide, wherein each of said first and second polypeptide comprises at least one immunoglobulin single variable domain (ISVD) and a C-terminal extension comprising a cysteine moiety (preferably at the C-terminus), wherein said first polypeptide and said second polypeptide are covalently linked via a disulfide bond between the cysteine moiety of said first polypeptide and the cysteine moiety of said second polypeptide, in which the dimer outperformed the benchmark constructs, e.g. cognate multivalent and multispecific constructs, in various assays. The present invention provides methods for making the dimers of the invention.

CYSTEINE LINKED NANOBODY DIMERS

The present invention relates to dimers comprising a first polypeptide and a second polypeptide, wherein each of said first and second polypeptide comprises at least one immunoglobulin single variable domain (ISVD) and a C-terminal extension comprising a cysteine moiety (preferably at the C-terminus), wherein said first polypeptide and said second polypeptide are covalently linked via a disulfide bond between the cysteine moiety of said first polypeptide and the cysteine moiety of said second polypeptide, in which the dimer outperformed the benchmark constructs, e.g. cognate multivalent and multispecific constructs, in various assays. The present invention provides methods for making the dimers of the invention.

Method for evaluating in vivo protein nutrition based on LC-MS-MS technique

Disclosed is a method for evaluating in vivo protein nutrition based on an LC-MS-MS technique, including the following steps: (1) collecting contents from different intestinal segments, and extracting and isolating protein ingredients; (2) determining the concentration of proteins; (3) treating before carrying out mass spectrometry: including digestion and desalting of a whole protein solution; (4) LC-MS-MS analysis; (5) database searching; and (6) data processing. Proteomic technology is used to identify proteins in the contents of different intestinal segments and digestive products thereof, and the source of the proteins in the contents of different intestinal segments and the contents thereof can be determined therefrom. Through bioinformatic analysis, the function of differential proteins in the body can be further understood, where the gene expression of enzymes related to protein digestion and metabolism may be different, thereby providing a scientific basis for further scientific evaluation of protein digestion and utilization.

Method for evaluating in vivo protein nutrition based on LC-MS-MS technique

Disclosed is a method for evaluating in vivo protein nutrition based on an LC-MS-MS technique, including the following steps: (1) collecting contents from different intestinal segments, and extracting and isolating protein ingredients; (2) determining the concentration of proteins; (3) treating before carrying out mass spectrometry: including digestion and desalting of a whole protein solution; (4) LC-MS-MS analysis; (5) database searching; and (6) data processing. Proteomic technology is used to identify proteins in the contents of different intestinal segments and digestive products thereof, and the source of the proteins in the contents of different intestinal segments and the contents thereof can be determined therefrom. Through bioinformatic analysis, the function of differential proteins in the body can be further understood, where the gene expression of enzymes related to protein digestion and metabolism may be different, thereby providing a scientific basis for further scientific evaluation of protein digestion and utilization.

METHODS FOR MANUFACTURING VIRAL VECTORS
20230212591 · 2023-07-06 · ·

The present disclosure provides improved systems and methods for purifying and/or concentrating lentiviral compositions.

METHODS FOR MANUFACTURING VIRAL VECTORS
20230212591 · 2023-07-06 · ·

The present disclosure provides improved systems and methods for purifying and/or concentrating lentiviral compositions.

SWEET PROTEIN MUTANTS FROM TRUFFLE

Newly identified fungal sweet-taste modifying proteins (designated Honey Truffle Sweetener (HTS)), and polynucleotides encoding the proteins are described. Specifically, Myd proteins with sweet taste modulation activity, and the cDNA encoding the same, are described, along with methods for isolating such cDNA and for isolating and expressing such proteins. Also disclosed are sweetening composition which includes the proteins of the invention, and methods to provide improved flavor to a product for oral administration.

SWEET PROTEIN MUTANTS FROM TRUFFLE

Newly identified fungal sweet-taste modifying proteins (designated Honey Truffle Sweetener (HTS)), and polynucleotides encoding the proteins are described. Specifically, Myd proteins with sweet taste modulation activity, and the cDNA encoding the same, are described, along with methods for isolating such cDNA and for isolating and expressing such proteins. Also disclosed are sweetening composition which includes the proteins of the invention, and methods to provide improved flavor to a product for oral administration.

Therapeutic immunoglobulin G4 for improved bioanalytical and bioprocessing properties

In certain embodiments, the disclosure provides an IgG4 antibody comprising a heavy chain and a light chain, wherein the heavy chain comprises: (a) a modified IgG4 CH1 region having a substitution of the lysine residue at position 196; or (b) a modified IgG4 hinge region having a substitution of the serine residue at position 217, the glycine residue at position 220, the proline residue at position 224 or the proline residue at position 225. Preferably, the IgG4 antibody further comprises a substitution of the serine residue at position 228 in the heavy chain hinge region.

Therapeutic immunoglobulin G4 for improved bioanalytical and bioprocessing properties

In certain embodiments, the disclosure provides an IgG4 antibody comprising a heavy chain and a light chain, wherein the heavy chain comprises: (a) a modified IgG4 CH1 region having a substitution of the lysine residue at position 196; or (b) a modified IgG4 hinge region having a substitution of the serine residue at position 217, the glycine residue at position 220, the proline residue at position 224 or the proline residue at position 225. Preferably, the IgG4 antibody further comprises a substitution of the serine residue at position 228 in the heavy chain hinge region.