Abstract: A linker peptide for constructing a fusion protein. The linker peptide comprises a flexible peptide and a rigid peptide. The flexible peptide consists of one or more flexible units. The rigid peptide consists of one or more rigid units. The flexible unit comprises two or more amino acid residues selected from Gly, Ser, Ala, and Thr. The rigid unit comprises a human chorionic gonadotropin ?-subunit carboxy-terminal peptide (CTP) bearing a plurality of glycosylation sites. The linker peptide can more effectively eliminate mutual steric hindrance of two fusion molecules, decreasing a reduction/loss of polymerization or activity resulting from improper folding of an active protein or a conformational change. On the other hand, the negatively charged, highly sialylated CTP can resist renal clearance, further prolonging a half-life of a fused molecule and enhancing bioavailability of a fused protein.

Abstract: A linker peptide for constructing a fusion protein. The linker peptide comprises a flexible peptide and a rigid peptide. The flexible peptide consists of one or more flexible units. The rigid peptide consists of one or more rigid units. The flexible unit comprises two or more amino acid residues selected from Gly, Ser, Ala, and Thr. The rigid unit comprises a human chorionic gonadotropin ?-subunit carboxy-terminal peptide (CTP) bearing a plurality of glycosylation sites. The linker peptide can more effectively eliminate mutual steric hindrance of two fusion molecules, decreasing a reduction/loss of polymerization or activity resulting from improper folding of an active protein or a conformational change. On the other hand, the negatively charged, highly sialylated CTP can resist renal clearance, further prolonging a half-life of a fused molecule and enhancing bioavailability of a fused protein.

Abstract: The invention provides an antibody and/or an antigen binding fragment that binds to NGF, and the amino acid sequences of the heavy chain and light chain variable regions of the antibody. The NGF antibody and/or its antigen binding fragment provided by the invention has high affinity for NGF and can effectively block the binding between NGF receptor and NGF. This antibody and/or its antigen binding fragment can inhibit the binding activity of NGF and its receptor in vitro, and is suitable for the treatment of pain diseases which are related to the haughty expression or increased expression of NGF.

Abstract: A highly glycosylated human blood-clotting factor VIII (FVIII) fusion protein, and a manufacturing method and application of same. The fusion protein comprises, from the N-terminus to the C-terminus, a human (FVIII), a flexible peptide connector, at least one rigid unit of a human chorionic gonadotropin ?-subunit carboxyl terminal peptide, and a half-life extending portion (preferentially selected from a human IgG Fc variant). The fusion protein has a similar level of biological activity as a recombinant (FVIII) and an extended in vivo half-life, thereby improving pharmacokinetics and drug efficacy.

Abstract: A hyperglycosylated recombinant human coagulation factor IX (FIX) fusion protein, a preparation method therefor, and use thereof. The fusion protein sequentially comprises, from N- to C-terminus, a human FIX, a flexible peptide linker, at least one human chorionic gonadotropin ? subunit carboxy-terminal peptide rigid unit, and a half-life extending moiety. The fusion protein has a biological activity similar to that of the recombinant FIX, an extended in vivo activity half-life, and reduced immunogenicity, so as to improve pharmacokinetics and pharmacodynamics.

Abstract: A linker peptide for constructing a fusion protein. The linker peptide comprises a flexible peptide and a rigid peptide. The flexible peptide consists of one or more flexible units. The rigid peptide consists of one or more rigid units. The flexible unit comprises two or more amino acid residues selected from Gly, Ser, Ala, and Thr. The rigid unit comprises a human chorionic gonadotropin ?-subunit carboxy-terminal peptide (CTP) bearing a plurality of glycosylation sites. The linker peptide can more effectively eliminate mutual steric hindrance of two fusion molecules, decreasing a reduction/loss of polymerization or activity resulting from improper folding of an active protein or a conformational change. On the other hand, the negatively charged, highly sialylated CTP can resist renal clearance, further prolonging a half-life of a fused molecule and enhancing bioavailability of a fused protein.

Abstract: Disclosed is a fusion protein of a mutated recombinant single-chain human coagulation factor VIII (FVIII), a preparation method therefor, and a use thereof. The fusion protein sequentially comprises, from an N-terminus to a C-terminus, a mutated single-chain human FVIII having a partially deleted B-domain, a flexible peptide linker, at least one rigid unit of a carboxyl-terminal peptide of a human chorionic gonadotropin beta subunit, and a half-life prolonging moiety (preferably an IgG Fc variant). The fusion protein has a similar biological activity to a recombinant FVIII, a prolonged active half life in vivo, and better stability in vitro and in vivo, and thus improves the pharmacokinetics and efficacy of the fusion protein.

Abstract: The invention provides an antibody and/or an antigen binding fragment that binds to NGF, and the amino acid sequences of the heavy chain and light chain variable regions of the antibody. The NGF antibody and/or its antigen binding fragment provided by the invention has high affinity for NGF and can effectively block the binding between NGF receptor and NGF. This antibody and/or its antigen binding fragment can inhibit the binding activity of NGF and its receptor in vitro, and is suitable for the treatment of pain diseases which are related to the haughty expression or increased expression of NGF.

Abstract: A linker peptide for constructing a fusion protein. The linker peptide comprises a flexible peptide and a rigid peptide. The flexible peptide consists of one or more flexible units. The rigid peptide consists of one or more rigid units. The flexible unit comprises two or more amino acid residues selected from Gly, Ser, Ala, and Thr. The rigid unit comprises a human chorionic gonadotropin ?-subunit carboxy-terminal peptide (CTP) bearing a plurality of glycosylation sites. The linker peptide can more effectively eliminate mutual steric hindrance of two fusion molecules, decreasing a reduction/loss of polymerization or activity resulting from improper folding of an active protein or a conformational change. On the other hand, the negatively charged, highly sialylated CTP can resist renal clearance, further prolonging a half-life of a fused molecule and enhancing bioavailability of a fused protein.

Abstract: A hyperglycosylated recombinant human coagulation factor IX (FIX) fusion protein, a preparation method therefor, and use thereof. The fusion protein sequentially comprises, from N- to C-terminus, a human FIX, a flexible peptide linker, at least one human chorionic gonadotropin ? subunit carboxy-terminal peptide rigid unit, and a half-life extending moiety. The fusion protein has a biological activity similar to that of the recombinant FIX, an extended in vivo activity half-life, and reduced immunogenicity, so as to improve pharmacokinetics and pharmacodynamics.

Abstract: A highly glycosylated human blood-clotting factor VIII (FVIII) fusion protein, and a manufacturing method and application of same. The fusion protein comprises, from the N-terminus to the C-terminus, a human (FVIII), a flexible peptide connector, at least one rigid unit of a human chorionic gonadotropin ?-subunit carboxyl terminal peptide, and a half-life extending portion (preferentially selected from a human IgG Fc variant). The fusion protein has a similar level of biological activity as a recombinant (FVIII) and an extended in vivo half-life, thereby improving pharmacokinetics and drug efficacy.

Abstract: A linker peptide for constructing a fusion protein. The linker peptide comprises a flexible peptide and a rigid peptide. The flexible peptide consists of one or more flexible units. The rigid peptide consists of one or more rigid units. The flexible unit comprises two or more amino acid residues selected from Gly, Ser, Ala, and Thr. The rigid unit comprises a human chorionic gonadotropin ?-subunit carboxy-terminal peptide (CTP) bearing a plurality of glycosylation sites. The linker peptide can more effectively eliminate mutual steric hindrance of two fusion molecules, decreasing a reduction/loss of polymerization or activity resulting from improper folding of an active protein or a conformational change. On the other hand, the negatively charged, highly sialylated CTP can resist renal clearance, further prolonging a half-life of a fused molecule and enhancing bioavailability of a fused protein.