40results about How to "Promotes proper folding" patented technology

The invention discloses a recombinant plasmid capable of expressing a soluble human papilloma virus 16 subtype L1 protein and an expression method thereof. The recombinant plasmid is constructed by inserting a human papilloma virus 16 subtype L1 gene and an SUMO label gene into an expression plasmid. According to the recombinant plasmid disclosed by the invention, the HPV16 L1 gene is optimized, so that the HPV16 L1 gene is more applicable to efficient expression of a target protein in an escherichia coli host; meanwhile, an Sumo label expression system is initially applied to fusion expression in escherichia coli, and the solubility of the target protein is further enhanced, so that the expressed target protein has higher activity. The expression method disclosed by the invention has the advantages that the target protein solubility expression efficiency is obviously improved, the product property is uniform and stable, the target protein expression quantity in a supernatant of a fermented disrupted bacterium liquid can reach 70Mug/ml, and the numerical value is obviously higher than yields of the target protein in other prokaryotic expression systems, so that the industrial production requirement is met.

The invention relates to a virus-like particle (VLP) of a recombined human papillomavirus (HPV) 33 and a preparation method of the virus-like particle. According to the specific technical key points, a polynucleotide gene segment of a new coded and recombined HPV33 L1 protein, a carrier containing the gene segment, a host cell comprising the carrier, an HPV33 L1 fusion protein translated and expressed by the gene segment, a pentamer and the VLP consisting of the pentamer are provided. The invention furthermore discloses applications of the pentamer, a VLP protein and a vaccine composition consisting of the pentamer and the VLP protein to the preparation of drugs for preventing HPV33 infection.

The invention relates to an expressing method and application of micromolecule thioesterase, in particular to recombinant expression of micromolecule thioesterase to escherichia coli, and applicationof micromolecule thioesterase to production of 10-hydroxy-2-caproleic acid intermediate product trans-2-caproleic acid. Escherichia coli ester acyl coenzyme A thioesterase gene ydiI is connected ontopET-28a plasmid containing a sumo label; the escherichia coli BL21(DE3) is transferred; the recombinant escherichia coli (containing pET-28a-ydiI)) is used; trans-2-caproleic acid is produced througha cell-free system.

The invention belongs to the technical field of genetic engineering, and specifically discloses a genetically engineered bacterium for expressing solubility pig gamma-interferonPoIFN-gamma and construction method and application of the genetically engineered bacterium. The genetically engineered bacterium for expressing solubility pig gamma-interferonPoIFN-gamma is Escherichia coil BL21(DE3) carrying recombinant plasmid Pet-32a(+)-PoIFN-gamma and plasmid pTf16-ParaB-tig simultaneously, wherein the PoIFN-gamma gene sequence in the recombinant plasmid Pet-32a(+)-PoIFN-gamma is SEQ ID NO.4, and the plasmid pTf16-ParaB-tig can express the molecular chaperone tig. The method disclosed by the invention is capable of improving the solubility and output of the pig gamma-interferon, simple in process and low in cost, and has good industrial application value.

The invention relates to a recombinant VLP of HPV31 and a preparation method thereof. Specifically, the invention discloses a novel polynucleotide gene segment coding recombinant HPV31 L1 protein, a vector containing the gene segment, a host cell containing the vector, HPV31 L1 fusion protein translated and expressed by the gene segment, a pentamer and a VLP composed of the pentamer; and the invention also discloses application of the pentamer, VLP protein and a vaccine composition composed of the pentamer and the VLP protein in preparation of drugs used for preventing HPV31 infection.

The invention belongs to the field of medicine and discloses recombinant antibacterial peptide, and a preparation method and an application of the recombinant antibacterial peptide. An amino acid sequence of the recombinant antibacterial peptide is as shown as SEQ ID NO: 1 (Sequence Identifier Number 1). The polypeptide has a better broad-spectrum antibacterial action and can be used for preparing an antibacterial medicine.

The invention relates to a recombinant human papilloma virus 52 virus-like particle and a preparation method of the recombinant human papilloma virus 52 virus-like particle. The specific technical point is that the invention provides a polynucleotide gene segment of a novel coded recombinant HPV52 L1 protein, a carrier comprising the gene segment, a host cell comprising the carrier, an HPV52 L1 fusion protein translated and expressed by the gene segment, a pentamer and a VLP comprising the pentamer. The invention further discloses application of the pentamer, the VLP protein and a vaccine composition comprising the pentamer and the VLP protein to the preparation of a medicine used for preventing HPV52 infection.

The invention belongs to the fields of medicine and bioengineering, and discloses an immunoregulation peptide, and a preparation method and application thereof. The amino acid sequence of the immunoregulation is disclosed as SEQ ID NO:1. The immunoregulation peptide has high T lymphopoiesis promoting function, and can be used for preparing T lymphopoiesis promoting drugs.

The invention discloses an escherichia coli soluble expression vector capable of efficiently obtaining recombinant protein. A hexahistidine label-flexible linker peptide-chitin binding domain-peptide-containing complex coding gene and a thioredoxin-hexahistidine label complex coding gene are placed in the same vector, the characteristics that the peptide-containing protein can realize self-cutting under the condition of change of temperature and pH and the thioredoxin can promote correct folding of protein containing more disulfide bonds are used, through affinity mediation of a hexahistidine label or a chitin binding domain, by using an affinity chromatographymethod, the target protein purificationefficiency and purity can be greatly improved, the problem that Escherichia coli gene engineering expression products form inclusion bodies easily is solved at a low cost, the application value is high, and the application range is wide.

The invention discloses a yeast engineering bacteria for producing trypsin in a high-yield manner and a construction method of the yeast engineering bacteria, belonging to the genetic engineering field. According to the constructed yeast engineering bacteria, trypsin of thioredoxin is blended at the front expression end, and four aspartic acids and lysine (D4K) are inserted between the thioredoxin and the trypsin; the trypsin amidase activity (BAPNA (nitroaniline)) is 47.4U/mL and the esterase activity (BAEE (N-benzoyl-L-arginine-ethylester)) is 2667U/mL, the problems of trypsinogen activation and low yield are solved, and the trypsin production method by the yeast engineering bacteria has the advantages of high yield, simplified process and industrial application convenience.

The invention aims to provide a modified duck circovirus Cap protein as well as a preparation method and application thereof, that is, 21-36 peptide fragments rich in arginine at the N-terminal of theduck circovirus Cap protein are deleted, and a universal T cell epitope is introduced into a deletion region to promote immunogenicity; the amino acid sequence of the obtained modified duck circovirus Cap protein is SEQ ID NO: 1, and one nucleotide sequence is SEQ ID NO: 2. The modified duck circovirus Cap protein gene is connected with an expression vector and then transferred into escherichia coli BL21 (DE3), efficient soluble expression of duck circovirus Cap protein is achieved, the expressed protein is spontaneously assembled into virus-like particles, and the particles can be used for development of products such as duck circovirus gene engineering subunit vaccine and yolk antibody.

The invention belongs to the technical fields of genetic engineering, molecular biology and other biology, and particularly relates to an efficient culture medium for expressing a soluble recombinantprotein by escherichia coli and a preparation method of the culture medium. The culture medium can improve the success rate and yield of expressing the soluble recombinant protein in cytoplasm by theescherichia coli; the efficient culture medium is selected from an M9 culture medium, basic ingredients such as sorbitol, ethanol, glucose and sucrose are added, magnesium sulfate and ampicillin are also added, IPTG is used as an inducer, and the efficient culture medium aims to increase the soluble expression of the foreign protein; the efficient culture medium is used to express the recombinantprotein, especially to express the soluble recombinant protein by the escherichia coli; and the culture medium can use escherichia coli BL-21 or DH5alpha strains as reaction bacteria, or K12 or origamiB escherichia coli strains as reaction bacteria.

The present invention relates to a method for expressing the HMGB1 A-box protein using the SUMO system, comprising the following steps: using a plasmid containing HMGB1 as a template, designing primers to amplify the A-Box domain, substituting the amplified target gene A-Box Cloned into the pSumo-Mut expression vector between Stu I and Hind III to obtain the pSumo-Mut-A-Box plasmid; use the recombinant plasmid to transform ArcticExpress ^TM (DE3) Prokaryotic host bacteria, using IPTG to induce expression of the target protein; sumo protease enzymatic hydrolysis to obtain high-purity A-Box protein. The invention has the advantages that: the HMGB1 A-box fusion protein is efficiently, stably and solublely expressed by using the SUMO expression system, and a mature protein with high purity can be obtained after cleavage by SUMO protease I, and no amino acid residue remains.