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81results about How to "Increased expression of soluble" patented technology
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Potent T cell modulating molecules
ActiveUS7820166B2Improve the level ofReduce and eliminate tumorSugar derivativesImmunoglobulins against cell receptors/antigens/surface-determinantsT cellBiology
The present invention relates to a polypeptide construct comprising at least one CDR3 region, wherein at least one of the at least CDR3 regions comprises at least one substitution in the amino acid sequence YYDDHY (SEQ ID NO.1) and wherein the at least one substitution comprises: in the first position of SEQ ID NO.1 a substitution from Y to H; in the second position of SEQ ID NO. 1 a substitution from Y to S, from Y to N, from Y to F or from Y to H; in third position of SEQ ID NO. 1 a substitution from D to N or from D to E; in the forth position of SEQ ID NO. 1 a substitution from D to Q, from D to A, from D to V, from D to E or from D to G; in the fifth position of SEQ ID NO. 1 a substitution from H to Q, from H to P, from H to Y, from H to R or from H to N; or in the sixth position a substitution from Y to N.
Owner:MICROMET AG
Production of a soluble native form of recombinant protein by the signal sequence and secretional enhancer
InactiveUS20090011995A1Efficient productionImprove efficiencyFungiNervous disorderBiotechnologyMembrane permeability
The present invention is drawn to a method for enhancing secretional efficiency of a heterologous protein using a secretional enhancer consisting of a modified signal sequence which comprises the N-region of a signal sequence and / or a hydrophobic fragment of the said signal sequence comprising the said N-region and / or the hydrophilic polypeptide. The method of the present invention can be used not only for production of recombinant heterologous proteins by inhibiting insoluble precipitation and enhancing secretional efficiency of the recombinant protein into the periplasm or the extracellular fluid and but also for transduction of therapeutic proteins by enhancing membrane-permeability of the recombinant protein using a strong secretional enhancer.
Owner:REPUBLIC OF KOREA (NAT FISHERIES RES & DEV INST)
Infectious bursal disease virus subunit antigen-containing vaccine composition, preparation method and application thereof
ActiveCN103849631AReduce formationIncreased expression of solubleViral antigen ingredientsVirus peptidesAntigenAdjuvant
The present invention provides an infectious bursal disease virus (IBDV) subunit antigen-containing vaccine composition, which contains an immune amount of recombinant VP2 protein and an adjuvant. According to the present invention, with the subunit gene engineering vaccine composition, the infectious bursal disease can be effectively prevented and controlled; and with the purification technology adopted by the recombinant antigen protein, the endotoxin content in the vaccine composition is significantly reduced, the side reaction of the chicken individuals is significantly reduced, and the safety of the vaccine is substantially increased.
Owner:PU LIKE BIO ENG
Method for producing isoprene by utilizing blue algae
ActiveCN103215315AIncrease productionEfficient expressionMicroorganism based processesIsomerasesIsomerasePlant Sources
The invention discloses a method for producing isoprene by utilizing blue algae, and the method comprises the following steps of: (1) expressing an isoprene synthetase coding gene derived from blue gum and an isoprene synthetase coding gene with an optimized codon in the blue algae; (2) applying the promotor of a cpc operon to express a mediate terpenoid synthetase coding gene contained in the blue algae; (3) enhancing the expression of an prenyl pyrophosphate isomerase coding gene; (4) expressing a fusion protein which contains a prenyl pyrophosphate isomerase and an isoprene synthetase; and (5) applying an SMUO tag to express a heterologous protein in the blue algae. The method disclosed by the invention can be used for carrying out genetic modification on the blue algae and expressing the isoprene synthetase (IspS) of a plant source in the blue algae, outstandingly increases the output of isoprene produced through the gene engineering blue algae through multiple methods, greatly widens the application range of the gene engineering blue algae by applying research results to express other heterologous proteins in the gene engineering blue algae and has wide industrial application prospect.
Owner:SHANGHAI RES & DEV CENT OF INDAL BIOTECH
Monooxygenase mutant and preparation method and application thereof
The invention relates to the technical field of genetic engineering, and particularly relates to a monooxygenase mutant and a preparation method and application thereof. The monooxygenase mutant is provided with any one of amino acid sequences as shown in formulas (I) and (II), wherein the amino acid sequence in the formula (I) reaches 80% consistency with the amino acid sequence as shown in SEQ ID NO.1; the amino acid sequence in formula (II) is obtained by modifying, substituting, decreasing or increasing one or some amino acid to 23 to 508 amino acid sites of the amino acid sequence as shown in SEQ ID NO.1; 1-34 amino acid is substituted; the mutant has the activity of monooxygenase. According to the method, a plurality of different sites, namely, 23-508 amino acid sites, are mutated; and the result shows that the mutants are capable of improving the activity, stability, soluble expression and selectivity of monooxygenase as well as decreasing the dosage of monooxygenase.
Owner:ASYMCHEM LAB TIANJIN
Tyrosine phenol lyase engineering bacteria, construction method and applications thereof
InactiveCN107325996AImprove expression efficiencyIncreased soluble expressionBacteriaMicroorganism based processesMaltoseTyrosine phenol-lyase
The invention provides tyrosine phenol lyase engineering bacteria, a construction method and applications thereof, wherein the engineering bacteria are identified as Escherichia coli, are named Escherichia coli MBP-TPL, are preserved in the China Center for Type Culture Collection on April 21, 2017, and have the preservation number of CCTCC NO: M 2017202, wherein the preservation address is Wuhan University, Wuhan, China. According to the present invention, the expression plasmid is constructed by integrally linking the tyrosine phenol lyase gene and the maltose binding protein gene so as to obtain the Escherichia coli MBP-TPL, wherein the expression plasmid can express the maltose binding protein and the tyrosine phenol lyase in the fused manner; and the activity of the fermentation unit bacterial amount of the tyrosine phenol lyase is high, and the soluble expression amount is high.
Owner:ZHEJIANG LVCHUANG BIOTECHNOLOGY CO LTD
Method for increasing soluble expression quantity of 4, 6-alpha-glucosyltransferase
InactiveCN112143722AIncreased expression of solubleSimple operation processBacteriaTransferasesLactobacillus fermentumCyclodextrin
The invention discloses a method for increasing the soluble expression quantity of 4, 6-alpha-glucosyltransferase, belongs to the technical field of protein engineering and fermentation engineering, and particularly relates to a method for increasing the soluble expression quantity of 4, 6-alpha-glucosyltransferase (GtfB) by adding betaine, maltose, beta-cyclodextrin, trehalose and sorbitol smallmolecular substances into a fermentation medium in a process of expressing 4, 6-alpha-glucosyltransferase (GtfB) derived from lactobacillus fermentum by respectively taking escherichia coli and bacillus subtilis as hosts. The total enzyme activity of fermentation is improved. An effective strategy is provided for efficient expression of 4, 6-alpha-glucosyltransferase (GtfB), the operation processis simple, the cost is low, the effect is remarkable, and a foundation is laid for industrial production.
Owner:JIANGNAN UNIV
Hypoglycemic polypeptide fused protein, structure and use of derivate thereof
InactiveCN101328221AIncreased expression of solubleImprove stabilityNervous disorderPeptide/protein ingredientsSolubilityBacillus coli
The invention relates to a structure and application of a hypoglycemic polypeptide fused protein and derivates thereof, belonging to the bioengineering technical field. The invention provides the technical proposal that: a fused polypeptide obtained obtains high solubility expression in a bacillus coli system through addition of special polypeptide sequences. The fused polypeptide and the derivatives thereof have high stability and activity compared with the natural hypoglycemic polypeptide, and can generate obvious hypoglycemic activity when people take or are injected a certain dosage.
Owner:CHINA PHARM UNIV
Glycosyltransferase mutant and method for catalytically synthesizing rebaudioside A by using same
ActiveCN112375750AIncreased expression of solubleImprove efficiencyBacteriaTransferasesSucrose synthetaseEnzyme system
The invention discloses a glycosyltransferase mutant and a method for catalytically synthesizing rebaudioside A by using the same. The amino acid sequence of original glycosyltransferase is SEQ ID NO:1. According to the experiment, Asn196, Asn78, Asn400, Asn69, Gln72, Gln198, Gln178, Gln160 and Thr319 are screened on the basis of prediction obtained by starting from surface residues Q, N and T ofUGT76G1 and combining data analysis results of solvent accessible surface area, B-factor and the like, and finally, a UGT-SuSy system of the better mutant strain 76G1_Q72E-N196D-T319E is screened outby virtue of single-point or multi-point iterative mutation in Thr81, so as to realize efficient catalytic synthesis of the rebaudioside A. The glycosyltransferase UGT76G1 or a mutant gene thereof isconnected with a sucrose synthase gene to obtain a recombinant plasmid, and a double-enzyme co-expressed recombinant strain is constructed. By constructing a double-enzyme system, regeneration of in-vivo UDPG is realized, the problem of sources of expensive glycosyl donors is effectively solved, the cost is reduced, and application of biotechnology industry is promoted. The mutant is simple to prepare, the rebaudioside A is synthesized through efficient catalysis in a short time, and the biological enzyme catalysis method is green, environmentally friendly and pollution-free and is more suitable for current green industrial processing and production.
Owner:NANJING UNIV OF TECH
Modified keto reductase mutant and preparation method and application thereof
ActiveCN108048416AHigh activityImprove stabilityOxidoreductasesGenetic engineeringGenetic engineeringAmino acid
The invention relates to the technical field of genetic engineering, in particular to modified keto reductase mutant and a preparation method and application thereof. The modified keto reductase mutant has any one of amino acid sequences shown in (I) and (II), to be specific, the amino acid sequence (I) is least 80% the same as that shown in SEQ ID NO. 1, and the amino acid sequence (II) is formedby subjecting amino acids 12 to 214 in the amino acid sequence of SEQ ID NO. 1 to modification, substitution, deletion or addition of one or more amid acids; the substitution refers to substitution of 1-14 amino acids, wherein the modified keto reductase mutant is active the same as keto reductase. By designing mutations for the multiple sites of amino acids 12 to 214, these mutations provide improved activity, stability, soluble expression and selectivity for keto reductase and also enables less keto reductase to be used.
Owner:JILIN ASYMCHEM LAB CO LTD
Preparation method of soluble recombinant proteins
InactiveCN109055416APurification is achieved quicklyAchieve purificationPeptide preparation methodsEnzymesSolubilityInclusion bodies
The invention discloses a preparation method of soluble recombinant proteins. According to the preparation method of the invention, a to-be-researched target protein and thioredoxin and His tag are expressed in a fusion manner, by optimizing an expression condition, the solubility expression amount of the target protein can be significantly improved, by utilizing the restriction enzyme cutting site characteristics of enterokinase, the purification of the target protein is rapidly realized by virtue of two-step affinity chromatography, and the purity can reach 95 percent or more. Compared withthe traditional method, by adopting the preparation method of the invention, the expression amount of the soluble recombinant protein can be significantly improved, the instability of the after-treatment renaturation and activity of an inclusion body protein can be avoided, the obtained recombinant protein is high in biological activity and relatively stable, and the application prospect for the mass production of the high-activity recombinant protein is good.
Owner:HENAN RADIOMEDICAL SCI & TECH CO LTD
Foreign protein soluble expression plasmid, preparation method thereof and application method thereof
InactiveCN101942478AIncreased expression of solubleRapid purificationVector-based foreign material introductionEscherichia coliForeign protein
The invention discloses a foreign protein soluble expression plasmid, a preparation method thereof and application method thereof, which belong to the technical field of bioengineering. The plasmid is pET30E, wherein the DNA sequence of the plasmid is presented by Seq ID No.1. An amplified product obtained by performing PCR amplification on a plasmid template and a primer group is connected with a pMD18-t vector; an Escherichia coli clone is obtained by transforming Escherichia coli DH5 alpha; and a product obtained by performing enzyme cutting connection on the Escherichia coli clone serving as a substrate is used for transforming the Escherichia coli DH5 alpha to form soluble expression plasmid molecules. The application method comprises the following steps that: the obtained expression plasmid molecules are used to transform Escherichia coli BL21 (DE3) competent cells through thermal activation to form a recombinant Escherichia coli colony; and after a bacteroid cell is obtained through inoculation culture, the soluble expression of the expression plasmid molecule is improved. The plasmid of the invention has promotion effect on assistance of the soluble expression of foreign proteins in Escherichia coli and has a great significance for further analysis of the functions of the proteins.
Owner:SHANGHAI JIAO TONG UNIV
Soluble expression increased bacillus pumilus W3 CotA laccase composite mutant
InactiveCN107034200AImprove performanceIncreased expression of solubleBacteriaMicroorganism based processesBacillus pumilusMutant
The invention discloses a soluble expression increased bacillus pumilus W3 Cota laccase composite mutant, and belongs to the field of biological engineering. The composite L386W / G417L / G57F(WLF)CotA laccase gene which is constructed at the early stage of the lab and has greatly improved catalyzing efficiency (ABTS is used as substrate) is used as a template to further mutate Asp on the 501 site of the composite mutant into Gly and Lys on the 317 site into Asn. The bacillus pumilus W3 CotA laccase mutant has a soluble expression which is 3.04 times that of WT-CotA and 3.63 times that of WLF, has a catalyzing efficiency whichis 4.6 times that of WT-CotA and 1.03 times that of WLF, and has excellent pH value and temperature stability. The CotA laccase mutant is more applicable to industrial application, and has a wide application prospect.
Owner:JIANGNAN UNIV
Recombinant escherichia coli and method for biosynthesizing diosmetin by utilizing recombinant escherichia coli
ActiveCN112725256AIncreased expression of solubleHigh catalytic activityBacteriaMicroorganism based processesEscherichia coliOrganosolv
The invention discloses recombinant Escherichia coli and a method for biosynthesizing diosmetin by using the recombinant Escherichia coli, the recombinant Escherichia coli is obtained by introducing a recombinant plasmid into host Escherichia coli, and the recombinant plasmid is constructed by connecting an encoding gene of AnFNSI after codon optimization and an expression vector pET-28a (+); The AnFNSI is flavone synthase 1 derived from angelica archang lica, the amino acid sequence of the AnFNSI is as shown in SEQ ID NO.1, and the amino acid sequence of the AnFNSI after codon optimization is as shown in SEQ ID NO.4. The recombinant Escherichia coli is used as a whole-cell catalyst to catalyze a substrate hesperetin to biosynthesize diosmetin. The method is green and efficient, does not need to use a large amount of organic solvents or toxic chemical reagents in the reaction process, and is low in cost, high in safety and easy for large-scale production.
Owner:HUNAN AGRI PRODS PROCESSING INST
Gene for encoding Cap protein of porcine circovirus 2 and application thereof
ActiveCN107337718AHigh expressionSolve the problem of low expressionBacteriaViral antigen ingredientsEscherichia coliPorcine circovirus
The invention provides a gene for encoding Cap protein of porcine circovirus 2, a recombinant expression vector containing the gene and a recombinant bacterium containing the recombinant vector. The gene expresses easily in escherichia coli and comprises a sequence shown in SEQ ID NO.1. The invention further provides a method for inducing the recombinant bacterium to produce the Cap protein of the porcine circovirus 2 and application in the aspect of utilizing the protein to produce a vaccine of the porcine circovirus 2. Through the adoption of the gene for encoding Cap protein of the porcine circovirus 2 and the application thereof, the full-length Cap protein can efficiently express in escherichia coli, the operation is simple, the cost is cost, and the large-scale production is easy to achieve; the recombinant bacterium and the vaccine have wide application prospects in preventing and controlling diseases of the porcine circovirus 2.
Owner:INST OF ANIMAL SCI & VETERINARY MEDICINE SHANDONG ACADEMY OF AGRI SCI
Genetically engineered bacteria of high-yield malto-oligosaccharide-based trehalose-hydrolyzing enzyme and application of genetically engineered bacteria
ActiveCN105969713AIncreased expression of solubleBacteriaMicroorganism based processesBiotechnologyTrehalose
The invention discloses genetically engineered bacteria of a high-yield malto-oligosaccharide-based trehalose-hydrolyzing enzyme and application of the genetically engineered bacteria and belongs to the technical field of genetic engineering and fermentation engineering. The genetically engineered bacteria pET-32a(+)-treZ / E.coli Origami(DE3) of the high-yield malto-oligosaccharide-based trehalose-hydrolyzing enzyme is constructed by taking E.coli Origami(DE3) as a host. The strain is used as a production strain and is fermented in a fermentation tank to generate the enzyme; and the activity of the enzyme can reach 204.U.mL<-1> and is about 4.9 times as much as that of shaking bottle fermentation. The production cost of the malto-oligosaccharide-based trehalose-hydrolyzing enzyme is reduced and a foundation is laid for industrial production of trehalose.
Owner:LIYANG WEIXIN CHEM
Recombinant expression vector for improving soluble expression of pathogenesis-related proteins in Mongolia astragaloside
PendingCN111733178AIncreased expression of solubleHas nuclease activityPeptide preparation methodsPlant peptidesEscherichia coliProtein target
The invention discloses a recombinant expression vector for improving soluble expression of pathogenesis-related proteins in Mongolia astragaloside. The recombinant expression vector is a recombinantpET30a-skp-AmPR-10 constructed by using pET30a as a vector and modifying AmPR-10 by utilizing an escherichia coli molecular chaperone skp. According to the invention, by a method of replacing the vector and carrying out molecular chaperone modification, the soluble expression of target proteins is improved so as to fulfill the aims of saving cost and improving yield; the exogenously expressed AmPR-10 is further subjected to activity measurement so as to show that the exogenously expressed proteins also have the nuclease activity and provide reference strategies for in-vitro expression of otherhomologous related proteins; and the activity may have the important significance for researching the RNA virus resistance ability of radix astragali.
Owner:SHANXI UNIV OF CHINESE MEDICINE
Bacillus pumilus W3 CotA laccase mutant with improved soluble expression
InactiveCN107227302AImprove performanceIncreased expression of solubleBacteriaWater contaminantsBacillus pumilusMutant
The invention discloses a Bacillus pumilus W3 CotA laccase mutant with improved soluble expression, belonging to the field of bioengineering. According to the invention, a composite mutant, i.e., L386W / G417L / G57F (WLF) CotA laccase gene, constructed in our laboratory in an early period and having greatly improved catalytic efficiency (with ABTS as a substrate) is used as a template, and Asp at the site 501 of the composite mutant is further mutated into Gly. The soluble expression level of the Bacillus pumilus W3 CotA laccase mutant provided by the invention is 3.75 times the soluble expression level of WT-CotA and 4.48 times the soluble expression level of WLF; the catalysis efficiency of the Bacillus pumilus W3 CotA laccase mutant is 4.4 times the catalysis efficiency of WT-CotA and 0.993 time the catalysis efficiency of WLF; and the Bacillus pumilus W3 CotA laccase mutant maintains good pH and temperature stability. The CotA laccase mutant obtained in the invention is more suitable for industrial application and has better application prospects.
Owner:JIANGNAN UNIV
Globular adiponectin variants
InactiveUS7592423B2Improve the level ofImprove solubilityObesity gene productsSugar derivativesSolubilityAmino acid
An adiponectin variant with one or more amino acid modifications relative to a corresponding parent adiponectin, wherein the adiponectin variant is not glycosylated, the adiponectin variant does not have residues 1-100 relative to human adiponectin, and wherein the solubility of the variant is improved by at least 3-fold relative to residues 110-244 of human adiponectin.
Owner:XENCOR INC
Method for producing human insulin growth factor-1 in recombinant Escherichia coli
InactiveCN101948837APromote formationIncreased expression of solubleBacteriaPeptide preparation methodsFusion Protein ExpressionEscherichia coli
The invention discloses a method for producing a human insulin growth factor-1 in recombinant Escherichia coli, which comprises: designing and synthesizing a gene associated with a hIGF-1 protein; constructing a hIGF-1 fusion protein expression vector; transforming an Escherichia coli host with the expression vector and constructing genetic engineering bacteria; expressing the hIGF-1 fusion protein by the genetic engineering bacteria; separating the hIGF-1 fusion protein; digesting the fusion lag of the hIGF-1 fusion protein by enterokinase; detecting the activity of the hIGF-1 by culturing NIH3T3 cells; and the like. In the invention, the fusion protein expressed in series is adopted, the N terminal of the fusion protein is thioredoxin, the C terminal of the fusion protein is hIGF-1, the middle of the fusion protein has 6 His lags, the expression product is more stable, the separation method is simple and cheap, and thus, the method has a promising application prospect.
Owner:ZHEJIANG UNIV
Plasmid for heterologous protein solubility expression and preparation and application method thereof
InactiveCN102533835AIncreased expression of solubleRapid purificationMicroorganism based processesVector-based foreign material introductionEscherichia coliRestriction enzyme digestion
The invention relates to a plasmid for heterologous protein solubility expression and a preparation and application method thereof. The plasmid is PET30e, and a deoxyribonucleic acid (DNA) sequence of the plasmid is described as Seq ID No.1. Amplification product obtained by conducting polymerase chain reaction (PCR) amplification on a plasmid template and primers is connected with a pMD18-T vector, clone of escherichia coli is obtained by transforming escherichia coli DH5 alpha and serves as a substrate to conduct restriction enzyme digestion and connection to obtain a product which transforms the escherichia coli DH5 alpha to obtain solubility expression plasmid molecules. The application method includes that the obtained expression plasmid molecules transform escherichia coli BL21 (DE3) competent cells to obtain a recombination escherichia coli bacterial colony in heat shock method, somatic cells are obtained through inoculation cultivation to obtain improvement of solubility expression. The plasmid for the heterologous protein solubility expression and the preparation and application method of the plasmid can improve solubility expression of the heterologous protein in the escherichia coli and have important meaning for further analyzing functions of the protein.
Owner:SHANGHAI JIAO TONG UNIV
Method for recombination, amalgamation and expression of series antimicrobial peptide gene
InactiveCN101319222AEfficient expressionHigh expressionVector-based foreign material introductionDNA/RNA fragmentationSolubilityFusion Protein Expression
The invention relates to a method for expressing a cascade antibacterial peptide gene by recombination and fusion. The multi-copy antibacterial peptide gene is expressed through the fusion with thioredoxin TrxA, thereby not only making use of the multiple copies to improve the proportion of a target polypeptide in an expression product, but also improving the expression amount of the cascade antibacterial peptide gene and promoting soluble expression through fusing protein, thereby overcoming the defects of low polypeptide proportion in the fusion protein by using a fusion expression single-copy antibacterial peptide gene method, and low expression amount and low solubility by using a direct cascade target polypeptide gene method. The method can realize the efficient expression of the cascade antibacterial peptide gene. Under optimal conditions, the total expression amount of the recombinant and fused antibacterial peptide exceeds 2mg / mL (extracting solution).
Owner:FEED RESEARCH INSTITUTE CHINESE ACADEMY OF AGRICULTURAL SCIENCES
Method for obviously improving soluble expression quantity of linoleate isomerase in recombinant escherichia coli
InactiveCN107988195AEasy to buildEasy to useCis-trans-isomerasesVector-based foreign material introductionRecombinant escherichia coliGroES
The invention discloses a method for obviously improving soluble expression quantity of linoleate isomerase in recombinant escherichia coli, and belongs to the field of genetic engineering. Accordingto the method, recombinant escherichia coli E.coli BL21(DE3)(pET-22b(+) / pai) is used as a starting strain; through co-expression of molecular chaperone proteins and assistance of the linoleate isomerase folding, soluble expression level of the linoleate isomerase is improved, so that enzyme activity of the linoleate isomerase is improved. Finally, a molecular chaperone system GroEL-GroES is preferably obtained, so that the enzyme activity of the linoleate isomerase is improved by 56 percent.
Owner:JIANGNAN UNIV
Construction of metallothionein fusion protein, rapid preparation of immobilized carrier and application of metallothionein fusion protein in heavy metal ion removal
ActiveCN110776571AIncreased expression of solubleIncrease productionOther chemical processesAntibody mimetics/scaffoldsEscherichia coliBULK ACTIVE INGREDIENT
The invention provides construction of metallothionein fusion protein, rapid preparation of an immobilized carrier and application of the metallothionein fusion protein in heavy metal ion removal. A genetic engineering method is used for fusing encoding genes of metallothionein, carbohydrate binding domain and superfolded green fluorescent protein to obtain a fusion gene mt-cbm-sfGFP. An expression vector is constructed from the fusion gene and transformed into an escherichia coli expression host to be expressed. The expressed protein is immobilized onto an insoluble carbohydrate carrier, andwater-insoluble carbohydrate particles bound with the metallothionein are further applied to remove heavy metal ions in traditional Chinese medicine flos lonicerae japonicae water decoction. The results show that lead ions can be removed quickly and effectively without affecting main active ingredients in the flos lonicerae japonicae water decoction. The method has the advantages of low cost, quickness and convenience and visualization, and can be used for the rapid and effective removal of heavy metals in traditional Chinese medicine water decoction, liquid food and waste water.
Owner:福建省中医药科学院
Method for improving soluble expression of microbial transglutaminase in escherichia coli
InactiveCN104087563AIncreased expression of solubleGood expressionBacteriaMicroorganism based processesGlutaminaseSolubility
The invention provides a method for improving soluble expression of microbial transglutaminase (MTG) in escherichia coli. According to the method, two plasmids, pET-MTG and pA-GESP are co-transformed into escherichia coli DE3, and microbial transglutaminase is solubly expressed in an induced supernantant. The pET system is utilized for efficiently expressing MTG, and also a molecular chaperone co-expression system is established, so that the solubility of a MTG expression product is improved, and results show that the method helps to improve the soluble expression of MTG in escherichia coli with obvious expression effect, and establishes a good base for industrialized production in future.
Owner:ANHUI BBCA FERMENTATION TECH ENG RES
Pharmaceutical compositions of adiponectin variants and methods of storage
InactiveUS7678886B2Improve the level ofImprove solubilityPeptide/protein ingredientsMetabolism disorderEndocrinologyDrug
A composition comprising an adiponectin variant at a concentration of at least 2.0 mg / mL, and a pharmaceutically acceptable carrier, wherein less than 20% of said adiponectin variant would aggregate after storage at 4° C. for one week in 10 mM PO4, 150 mM NaCl buffer.
Owner:XENCOR INC
Recombinant protein for detecting tri-methylated modification of histone locus and application thereof
ActiveCN107312096AQuality improvementIncreased expression of solubleMicroorganism based processesDepsipeptidesWestern blotAntibody
The invention provides a recombinant protein for detecting tri-methylated modification of a histone locus and application thereof. An amino acid sequence of the recombinant protein comprises an N-terminal GST fusion protein sequence and a C-terminal Tudor structural domain sequence which are connected in series. The recombinant protein provided by the invention has high affinity to H3K4 and H4K20, can be used for replacing a commercialized antibody to perform Western Blot experiment, is high in sensitivity, has no cross linking; the production cost is remarkably reduced, the batch quality is extremely stable, and the batch production can be realized quickly.
Owner:HUBEI UNIV
Expression control of TrxA, encoding zone gene, its prepn. and uses
InactiveCN1834246AOvercome incompatibilitiesEasy to operateFermentationVector-based foreign material introductionThioredoxinPlasmid
This invention relates to the manufacture and application of the expression regulating and encoding region gene of Escherichia coli thioredoxin (TrxA). The gene is manufactured by: cloning the expression regulating and encoding region of TrxA by PCR technique that has the basic group sequence in SEQ ID No.1, and cloning it the the upstream of pET-28a promoter to promote the soluble expression of heterologous protein in Escherichia coli. The results show that TrxA and heterologous protein can combine to coexpress in non-fusion mode in Escherichia coli BL21 (DE3), and can promote the solubility of heterologous protein.
Owner:SHENYANG INST OF APPLIED ECOLOGY - CHINESE ACAD OF SCI
Preparation and application of human superoxide dismutase hSOD1 mutant
The invention provides a preparation method and application of a human superoxide dismutase hSOD1 mutant, and relates to the technical field of bioengineering. The invention provides a coding protein of a human-derived superoxide dismutase hSOD1 mutant, wherein the coding protein has an amino acid sequence shown as SEQ ID NO.Mt1SOD1aa; the invention provides an Mt1SOD1 gene for coding the protein, and the Mt1SOD1 gene has a nucleotide sequence as shown in SEQ ID NO.Mt1SOD1. According to the invention, human-derived hSOD1 is taken as a template, an hSOD1 mutant Mt1SOD1 (E25G, P29T, E101V and C112S) gene is obtained through gene mutation, and human-derived superoxide dismutase hSOD1 mutant Mt1SOD1 protein is recombined; and the heterologous problem is solved in application. And the polypeptide has high activity and high stability, and provides a new way for the development of novel functional anti-aging cosmetics and series products and the development of other anti-aging products such as functional foods and anti-aging drugs.
Owner:SOUTHWEST JIAOTONG UNIV
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