Abstract: The present invention relates to an antibody that recognizes a specific motif of WLS protein so as to inhibit overactivation of the Wnt signaling pathway to thereby prevent or treat a disease associated with the Wnt signaling pathway, and to a pharmaceutical composition containing the same.
Type:
Application
Filed:
August 26, 2015
Publication date:
November 2, 2017
Applicant:
Atgen Co., Ltd.
Inventors:
Ho Geun Yoon, Jae Ho Cheong, Eun Sung Park, Jae Sung Seo, Hyun Jung Kee
Abstract: The present invention relates to peptides comprising at least one sequence selected from the group consisting of oligopeptide sequences of at least about 10 but not more than about 50 continuous amino acid residues in the amino acid sequence of the C-terminal acidic tail (ATS), which can render fusion partner proteins environmental stress resistant by binding thereto while conserving their intrinsic properties. Also, it relates to fusion proteins formed by binding the above peptides to fusion partner proteins, nucleotide sequences encoding said fusion proteins, recombinant vectors comprising said nucleotide sequences, and cells transformed or transfected with said recombinant vectors. In addition, it relates to processes for producing the above environmental stress resistance conferring peptides or environmental stress resistant fusion proteins by chemical synthesis or genetic recombination.
Abstract: The present invention relates to a peptide capable of conferring resistance to environmental stresses, comprising a peptide fragment containing a sequence composed of 10 or more consecutive amino acid residues including five or more acidic amino acid residues, wherein the peptide fragment is derived from the C-terminal acidic tail of synuclein, or its derivative, and to a fusion protein comprising the peptide and a fusion partner protein being linked to the peptide, wherein the fusion protein is resistant to environmental stresses. Also, the present invention is concerned with a method of conferring resistance to environmental stress to a protein of interest, comprising linking the protein to the peptide. While maintaining the intrinsic properties of the fusion partner protein, the fusion protein is resistant to environmental stresses, including heat, pH, metal ions, repeated freezing/thawing and high-concentration of polypeptide.
Abstract: The present invention relates to peptides comprising at least one sequence selected from the group consisting of oligopeptide sequences of at least about 10 but not more than about 50 continuous amino acid residues in the amino acid sequence of the C-terminal acidic tail (ATS), which can render fusion partner proteins environmental stress resistant by binding thereto while conserving their intrinsic properties. Also, it relates to fusion proteins formed by binding the above peptides to fusion partner proteins, nucleotide sequences encoding said fusion proteins, recombinant vectors comprising said nucleotide sequences, and cells transformed or transfected with said recombinant vectors. In addition, it relates to processes for producing the above environmental stress resistance conferring peptides or environmental stress resistant fusion proteins by chemical synthesis or genetic recombination.
Abstract: The present invention relates to peptides comprising at least one sequence selected from the group consisting of oligopeptide sequences of at least about 10 but not more than about 50 continuous amino acid residues in the amino acid sequence of the C-terminal acidic tail (ATS), which can render fusion partner proteins environmental stress resistant by binding thereto while conserving their intrinsic properties. Also, it relates to fusion proteins formed by binding the above peptides to fusion partner proteins, nucleotide sequences encoding said fusion proteins, recombinant vectors comprising said nucleotide sequences, and cells transformed or transfected with said recombinant vectors. In addition, it relates to processes for producing the above environmental stress resistance conferring peptides or environmental stress resistant fusion proteins by chemical synthesis or genetic recombination.