Abstract: A DNA sequence encoding Der p1 protein having a particular base sequence is codon-optimized for the Pichia pastoris expression system, which is conducive to expressing Der p1 in Pichia pastoris. After gene optimization and adding an activating element to increase the expression of Der p1 in molecular level, it was found that Der p1 is expressed at a higher level as compared with the prior art and has biological activity similar to the natural protein.

Abstract: A DNA sequence encoding Der p2 protein having a particular base sequence is codon-optimized for the Pichia pastoris expression system, which is conducive to expressing Der p2 in Pichia pastoris. After gene optimization and adding an activating element to increase the expression of Der p2 in molecular level, it was found that Der p2 is expressed at a higher level as compared with the prior art and has biological activity similar to the natural protein.

Abstract: Provided are an optimized Der f2 gene, a recombinant Der f2 protein encoded thereby, a vector comprising said gene, and a Pichia pastoris strain. Also provided are an expression method, a purification method, and an application of the recombinant Der f2 protein.

Abstract: The present application discloses a PEGylated asparaginase and use thereof. In this application, the polyethylene glycol (PEG) is coupled to the N-terminal amino of 1 or 2 subunits of L-asparaginase, and the molecular weight of the PEG is 30-40 KDa. The PEG is preferably branched and has an aldehyde serving as an activating group. The PEGylated asparaginase is useful in the preparation of anti-tumor drugs.

Abstract: Provided are an optimized proDer f1 gene, a proDer f1 protein encoded thereby, a vector comprising said gene, and a Pichia pastoris strain. Also provided are an expression method and a purification method of the proDer f1 protein.

Abstract: The present application discloses a PEGylated asparaginase and use thereof. In this application, the polyethylene glycol (PEG) is coupled to the N-terminal amino of 1 or 2 subunits of L-asparaginase, and the molecular weight of the PEG is 30-40 KDa. The PEG is preferably branched and has an aldehyde serving as an activating group. The PEGylated asparaginase is useful in the preparation of anti-tumor drugs.

Abstract: Provided are a recombinant group 2 allergen protein from Dermatophagoides pteronyssinus, and an encoding gene and preparation method thereof. The encoding gene is obtained by preforming codon optimization on a wild-type encoding gene of a group 2 allergen protein from Dermatophagoides pteronyssinus and is beneficial to expression in Pichia pastoris. Further, an acting element increasing target protein expression is added to the expression system.

Abstract: A DNA sequence encoding Der p1 protein having a particular base sequence is codon-optimized for the Pichia pastoris expression system, which is conducive to expressing Der p1 in Pichia pastoris. After gene optimization and adding an activating element to increase the expression of Der p1 in molecular level, it was found that Der p1 is expressed at a higher level as compared with the prior art and has biological activity similar to the natural protein.

Abstract: The present application discloses a PEGylated asparaginase and use thereof. In this application, the polyethylene glycol (PEG) is coupled to the N-terminal amino of 1 or 2 subunits of L-asparaginase, and the molecular weight of the PEG is 30-40 KDa. The PEG is preferably branched and has an aldehyde group serving as an activating group. The PEGylated asparaginase is useful in the preparation of anti-tumor drugs.

Abstract: Provided are an optimized proDer f1 gene, a proDer f1 protein encoded thereby, a vector comprising said gene, and a Pichia pastoris strain. Also provided are an expression method and a purification method of the proDer f1 protein.

Abstract: Provided are an optimized Der f2 gene, a recombinant Der f2 protein encoded thereby, a vector comprising said gene, and a Pichia pastoris strain. Also provided are an expression method, a purification method, and an application of the recombinant Der f2 protein.

Abstract: Methods for use of a multi-arm polyethylene glycol (PEG) modifier in modification of asparaginase. The described multi-arm PEG modifier enhances the subunit interaction of a multimeric protein to maintain the multimeric protein in a polymerized form, thereby improving the stability of the multimeric protein, maintaining the bioactivity of the multimeric protein, and reducing the probability of exposure of the antigen binding site after depolymerization of the subunits, so as to reduce the immunogenicity.

Abstract: The present invention relates to polyethylene glycol (PEG) modified protein drugs, and a PEGylated tissue kallikrein, a preparation method and use thereof are disclosed. The tissue kallikrein has a sequence as shown in SEQ ID No. 1 or SEQ ID No. 2, and the tissue kallikrein may be natural or recombinant. The PEG has a molecular weight of 20 to 40 kDa, and is conjugated to the N-terminal primary amino of the tissue kallikrein. In addition to the advantages of significantly extended half-life, significantly reduced immunogenicity and stable and uniform structure, the biological activity of the PEGylated KLK1 provided in the present invention is improved to a higher extent, which is more significant in the treatment of cerebral apoplexy and diabetic nephropathy in particular.

Abstract: The present application discloses a PEGylated asparaginase and use thereof. In this application, the polyethylene glycol (PEG) is coupled to the N-terminal amino of 1 or 2 subunits of L-asparaginase, and the molecular weight of the PEG is 30-40 KDa. The PEG is preferably branched and has an aldehyde group serving as an activating group. The PEGylated asparaginase is useful in the preparation of anti-tumor drugs.

Abstract: The present invention relates to polyethylene glycol (PEG) modified protein drugs, and a PEGylated tissue kallikrein, a preparation method and use thereof are disclosed. The tissue kallikrein has a sequence as shown in SEQ ID No. 1 or SEQ ID No. 2, and the tissue kallikrein may be natural or recombinant. The PEG has a molecular weight of 20 to 40 kDa, and is conjugated to the N-terminal primary amino of the tissue kallikrein. In addition to the advantages of significantly extended half-life, significantly reduced immunogenicity and stable and uniform structure, the biological activity of the PEGylated KLK1 provided in the present invention is improved to a higher extent, which is more significant in the treatment of cerebral apoplexy and diabetic nephropathy in particular.

Abstract: Methods for use of a multi-arm polyethylene glycol (PEG) modifier in modification of asparaginase. The described multi-arm PEG modifier enhances the subunit interaction of a multimeric protein to maintain the multimeric protein in a polymerized form, thereby improving the stability of the multimeric protein, maintaining the bioactivity of the multimeric protein, and reducing the probability of exposure of the antigen binding site after depolymerization of the subunits, so as to reduce the immunogenicity.