Zonhon Biopharma Institute, Inc

Gensun Institute of Biomedicine Co., Ltd.

Bruce Yong Ma

Jun Wang

Anliang Wang

Yu Fan

Chunlin Xu

Yaofang Wang

He Wang

Yifei Chen

Dinglong Wu

Chen Chen

Jing Qiu

A DNA sequence encoding Der p1 protein having a particular base sequence is codon-optimized for theexpression system, which is conducive to expressing Der p1 in. 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.

Variant recombinant dermatophagoides pteronyssinus type 1 allergen protein and its preparation method and application

A DNA sequence encoding Der p2 protein having a particular base sequence is codon-optimized for theexpression system, which is conducive to expressing Der p2 in. 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.

Recombinanttype 2 allergen protein and its preparation method and application

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

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.

Site-specific polyethylene glycolylated (pegylated) asparaginase, preparation method therefor and use thereof

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

Recombinanttype 1 allergen protein and its preparation method and application

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.

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.

Use of multi-arm polyethylene glycol modifier and application of multi-arm polyethylene glycol modifier in L-asparaginasum modification

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.

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Jiangsu, China

Bruce Yong Ma