38 results about "Serine protease" patented technology

To provide an antigen-binding protein comprising an antigen-binding domain that binds to plasmin. Also provided are compositions comprising the antigen binding proteins, as well as uses thereof and methods of treatment comprising the same.SOLUTION: To provide antigen-binding proteins or antigen-binding fragments thereof that specifically bind to the serine protease domain of plasmin and inhibit or reduce plasmin activity via interaction with the catalytic site of the protein.SELECTED DRAWING: None

This invention discloses a highly efficient serine protease for degrading α-keratin, its degradation method, and its applications. The serine protease is named PliKerS, and its full-length amino acid sequence is shown in SEQ ID No. 2, with the corresponding coding gene sequence shown in SEQ ID No. 1. The amino acid sequence of the recombinant serine protease rPliKerS, which has its N-terminal signal peptide removed and a purification tag attached to its C-terminus, is shown in SEQ ID No. 4, with the corresponding coding gene sequence shown in SEQ ID No. 3. The recombinant serine protease rPliKerS degrades α-keratin under mild conditions, avoiding the environmental burden of strong alkaline treatment. It is particularly suitable for applications involving pet hair, hair waste, and leather pretreatment. The degradation products are soluble proteins and peptides, which can be used as high-value-added amino acid raw materials, functional peptide raw materials, biodegradable materials, bio-based material precursors, bio-feed proteins, fertilizers, etc., exhibiting high resource utilization value and promising industrial application prospects.

The invention belongs to the technical field of biological medicines, and particularly relates to application of ackermania muciniphila and recombinant trichina serine protease carried by a derivative of the ackermania muciniphila to preparation of a medicine for treating intestinal inflammation symptoms. According to the present invention, the ackermann muciniphila and the ackermann muciniphila derivative carrying recombinant trichina serine are firstly disclosed, such that the physical barrier of the intestinal mucosa is repaired through the synergistic effect, the expression of TNF-alpha, IL-6, IL-1beta and other proinflammatory factors is specifically regulated and inhibited, the intestinal flora structure is remodeled, and the intestinal inflammation state is significantly improved; experimental results show that the Ackerman muciniphila and the derivative thereof carrying the recombinant trichina serine protease can significantly relieve weight loss of mice with intestinal inflammation induced by DSS, reduce DAI score, and reverse the phenomena of shortened colon and abnormal swelling of spleen. According to the invention, the probiotics and the parasite-derived protein are combined, so that the method has the advantages of high efficiency, safety and easiness in large-scale production, and a new biological preparation strategy is provided for accurate treatment of IBD.

The application discloses a latex-enhanced immunoturbidimetric detection reagent and application of a serine protease in the latex-enhanced immunoturbidimetric detection reagent, relates to the technical field of biological detection, and can reduce the interference of a matrix component on the binding of a target and an antibody, reduce the probability of non-specific binding, and improve the accuracy of detection by pretreating a to-be-detected sample by using a reagent R1 containing the serine protease; the difference between a sample matrix and a quality control product matrix can be avoided, the accuracy and reliability of a detection result are improved; the difference between different quality control product matrices can be eliminated, the difference between standard curves obtained by using different matrix quality control products is reduced, and the compatibility of three-party quality control is enhanced.

It provides an inhibitor of complement activation. [Solution] An isolated monoclonal antibody and its antigen-binding fragment are provided that specifically bind to an epitope within the serine protease domain of human MASP-2. In some embodiments, the antibody or its antigen-binding fragment inhibits lectin pathway complement activation. Polynucleotides encoding the monoclonal antibody or its antigen-binding fragment, and cloning vectors or expression cassettes containing such polynucleotides are also provided. Methods for inhibiting lectin pathway complement activation and methods for treating diseases and disorders of the lectin pathway are further provided.

This application relates to a wastewater treatment device for the preparation of recombinant plasmids of serine protease, comprising, in sequence: an inactivation module, a chemical pretreatment process, and a biodegradation process; the inactivation module includes: a pre-inactivation collection tank for receiving wastewater; a heat exchange device for heating the wastewater with high-temperature steam; and an inactivation tank for inactivation operations through heat preservation and pressure maintenance; the heat exchange device includes: a heat exchange cylinder with a shell and tube containing high-temperature steam and connecting the pre-inactivation collection tank and the inactivation tank; a cleaning mechanism for scraping the tube wall by rotation; and a power mechanism for converting the kinetic energy of the fluid inside the heat exchange cylinder into the power for the rotation of the cleaning mechanism. This application automatically cleans the scale and fouling on the inner wall of the heat exchange cylinder, and can also clean the heat exchange cylinder in a cold state, ensuring an extended service life and increased efficiency of the heat exchange cylinder during wastewater treatment.

The present invention relates to a genetically modified plant or plant cell derived from a wild-type plant or plant cell, said wild-type plant or plant cell producing at least one serine protease comprising the motif SSRGPX1LKPDX2X3APGX4SGTSMSCPHX5PX6WSPX7AX8X9SAX10MTT (SEQ ID No. 1), whereinX1 is a peptide consisting of 7 amino acid residues, X2 is I or L, X3 is T or M, X4 is a peptide consisting of 27 or 28 amino acid residues, X5 is a peptide consisting of 12 amino acid residues, X6 is T or E, X7 is S or A, X8 is V or I, X9 is K or R and X10 is I or M, wherein the proteolytic activity of the at least one serine protease in the genetically modified plant or plant cell is reduced compared to its activity in the wild-type plant or plant cell, wherein the genetically modified plant or plant cell comprises at least one exogenous nucleic acid molecule encoding for at least one protein or polypeptide of interest.

The invention relates to the technical field of marine technology and enzyme, and particularly discloses alkaline serine protease and application thereof. The brand-new alkaline serine protease is successfully mined by using a marine-derived microbial metagenome database, the limitation of conventional microbial isolated culture is overcome, and the source selection range of the alkaline serine protease is greatly widened. Moreover, the alkaline serine protease has excellent protease activity and detergent tolerance, and can be effectively used for protein degradation or used as a detergent component.

The invention discloses a sweet protein homotrimer as well as a preparation method and application thereof, and belongs to the technical field of genetic engineering. According to the technical scheme, the strategy of self-assembly of interchain disulfide bonds mediated by a PCA trimerization structural domain is adopted, the PCA trimerization structural domain is derived from a C-terminal fragment of snake venom serine protease, a stable homotrimer is spontaneously formed through the interchain disulfide bonds under the oxidation condition, and the stable homotrimer is used as an artificial trimerization'molecular rivet '; the PCA trimerization structural domain fragment is fused with sweet protein, controllable trimer assembly can be achieved in cells and / or outside cells, and no extra cross-linking agent is needed. Based on this, a sweet protein homotrimer is obtained from a sweet protein monomer; the sweet protein homotrimer has good thermal stability and pH tolerance, and a new technical platform is provided for industrial production of high-sweetness and high-stability functional protein.

The application belongs to the field of biological medicine and protein engineering, and particularly relates to a preparation method of a proteinase cryo-EM sample and a structural analysis method of the proteinase. The preparation method comprises the following steps: providing an enzyme solution of a target proteinase, adding an enzyme inhibitor of the target proteinase, collecting an incubation product supernatant after the obtained mixture is incubated, and preparing a cryo-EM sample by sucking the incubation product supernatant; the target proteinase comprises a serine protease, the target proteinase is located on a cell membrane, and / or the target proteinase is dependent on ATP. The application prepares a cryo-EM sample after the enzyme solution of the target proteinase is incubated by adding the enzyme inhibitor of the target proteinase, so that the problems of depolymerization of a membrane proteinase and instability of a protein soluble region can be overcome, the cryo-EM structure of a full-length membrane proteinase is successfully analyzed in electron microscope observation, and a precise reference is provided for subsequent design of specific targeted drugs.

This invention provides a method and composition for preparing a composition derived from Carica papaya. [Solution] A method is provided for preparing a composition derived from the fruit of the Carica papaya plant, wherein the composition has a pH of about 7.5 to 9.5, and the method comprises the steps of treating ripe fruit pulp of the Carica papaya plant with alkali without subjecting it to a heating step, and separating soluble proteases from insoluble plant material after the alkali treatment. A composition is also provided comprising one or more serine proteases of proteolytic activity obtainable by the method.

This invention relates to an expression vector, engineered bacteria, and method for inducing expression of a serine protease. The expression vector contains a nucleic acid sequence encoding a serine protease, and the amino acid sequence of the serine protease includes the sequence shown in SEQ ID NO.1. This invention transforms the expression vector into a host bacterium and utilizes its unique high-efficiency expression system for protein expression. By optimizing culture and induction conditions, high-efficiency expression of the serine protease was successfully induced. This serine protease exhibits highly efficient hydrolytic ability, with an enzyme activity reaching 925 U / mL.

The application discloses application of serine protease AprE and a coding gene thereof in prevention and treatment of rice blast, and belongs to the technical field of biotechnology.The amino acid sequence of the serine protease AprE is shown as SEQ ID NO.13, and the nucleotide sequence of the coding gene is shown as SEQ ID NO.14.It is found by the application that after the serine protease encoded by the aprE gene is used to treat blast fungus hypha cells, abnormal ROS accumulation occurs in the cells, and the hypha cells are caused to be apoptotic, broken and abnormally expanded, so that the pathogenic bacteria are finally killed.The aprE gene can be used to study biochemical nature of inhibition of the blast fungus, and can also be used as a target gene of a high-efficiency biocontrol strain and applied to biological prevention and treatment of rice blast.The recombinant serine protease can also be directly used for prevention and treatment of rice blast and reduction of pathogenicity of pathogenic bacteria.

The present application relates to a serine protease for selectively degrading mucin and use thereof. The serine protease is serine protease EatA, and the protein thereof comprises a passenger domain with serine protease EatA activity. The passenger domain has an amino acid sequence with at least 90% identity with SEQ ID NO. 2, and is preferably an amino acid sequence set forth in SEQ ID NO. 2. The serine protease EatA can selectively degrade mucin in disease-related mucus, and has relatively high and lasting stability.

This invention discloses a highly efficient serine protease for degrading β-keratin, its degradation method, and its applications. The serine protease is named LteKerS, and its amino acid sequence is shown in SEQ ID No. 2, while the corresponding coding gene sequence is shown in SEQ ID No. 1. The amino acid sequence of the recombinant serine protease rLteKerS, which has its N-terminal signal peptide removed and has a purification tag at its C-terminus, is shown in SEQ ID No. 4, while the corresponding coding gene sequence is shown in SEQ ID No. 3. The recombinant serine protease rLteKerS can efficiently degrade β-keratin under alkaline conditions, directly acting on intact feathers. The reaction conditions are mild, requiring no high temperature, high pressure, or complex pretreatment. The degradation products are soluble proteins and peptides, which can be used as high-value-added amino acid raw materials, functional peptide raw materials, biodegradable materials, bio-based material precursors, bio-feed proteins, fertilizers, etc. It is suitable for the large-scale processing of by-products such as poultry feathers and has good industrial application prospects.

The present invention relates to the treatment of physiologic iron overload and provides antibodies against the proteolysis 2 (MTP-2). Inhibition of MTP-2 reduces dietary iron uptake and reduces iron release from cellular stores in the body. Inhibitors of MTP-2, such as antibodies against the serine protease domain, are useful in the treatment of iron overload, which is characteristic of diseases such as beta-thalassemia and which would otherwise lead to toxic accumulation of iron. Combinations of MTP-2 inhibitors with activin receptor ligand traps or with erythropoietin provide additional therapeutic effects.

A water-soluble unit dose detergent article including a water-soluble film and a laundry liquid detergent composition, wherein the detergent composition includes:a non-soap surfactant system comprising anionic non-soap surfactant and nonionic surfactant wherein the anionic non-soap surfactant includes at least 80%, preferably at least 90% by weight of the anionic non-soap surfactant of linear alkyl benzene sulphonate; up to 15% by weight of the composition of water;a serine protease;a metalloprotease; andwherein the weight ratio of non-soap anionic surfactant to non-ionic surfactant is greater than 1.5:1.

The application discloses a protease with mild keratolysis, a composition and application, and belongs to the technical field of genetic engineering or cosmetics. The application provides a basic heat-stable serine protease TVG06 obtained in an acidic hot spring in Ali uninhabited area, and the amino acid sequence of the basic heat-stable serine protease TVG06 is shown as SEQ ID NO. 1. The serine protease in the application has a degradation rate of enzyme activity of less than 15% under the condition of 45 DEG C for 4 weeks, and the enzyme activity is more than 65% after 8 weeks. Compared with traditional keratolysis raw materials, the composition in the application has better oil control, anti-inflammatory and keratolysis effects, and is more soothing.

The invention relates to a pair of protein markers for diagnosing type 2 diabetes mellitus and application thereof, and belongs to the technical field of biological medicine. The invention identifies a pair of protein markers for diagnosing type 2 diabetes mellitus (T2DM), wherein the protein markers comprise HtrA serine protease 1 (HTRA1) and renal tubular interstitial nephritis antigen-like 1 (TINAGL1). The expression level of the protein marker has significant difference between type 2 diabetes patients and healthy control people. A random forest prediction model constructed on the basis of HTRA1 and TINAGL1 shows excellent discrimination performance, in an independent verification set, the area under a subject characteristic working curve is 0.992, and under the optimal cutoff value, the diagnosis sensitivity is 0.917, and the specificity is 1.000. The protein marker provided by the invention provides a brand new tool for noninvasive and early diagnosis of T2DM and high-risk population screening, and has important transformation application value.

The application relates to the fields of marine technology and enzyme technology, and particularly discloses a kind of alkaline serine protease and application thereof.A kind of brand-new alkaline serine protease is successfully mined by using marine-derived microorganism metagenome database, the limitation of conventional microorganism separation culture is overcome, and the source selection range of alkaline serine protease is greatly widened.Moreover, the alkaline serine protease has excellent protease activity and detergent tolerance, and can be effectively used for protein degradation or used as a detergent component.

The invention discloses a wheat peptide with muscle and weight gaining effects, a composition containing the wheat peptide as well as a preparation method and application of the wheat peptide, and relates to the technical field of food processing. The wheat peptide with the muscle and weight gaining effect is obtained by performing enzymolysis on wheat protein by adopting serine protease, trypsin and flavourzyme and then adding papain for enzymolysis. The wheat peptide can promote myoblast proliferation, improve the holding power and weight of mice, and effectively improve the relative level of IGF-1 in serum. In addition, the vitamin B6 and the vitamin B6 can cooperate to promote the absorption of whey protein.

The present disclosure reports that a calcium-dependent serine protease, complement component is (C1s) has been identified as a protease responsive for cleavage of exogenous polypeptides expressed in mammalian cell lines such as CHO cells. These CHO cell lines provide for increased yield of antigenically correct, uncleaved exogenous polypeptide as compared to unmodified CHO cells expressing the active C1s protease. C1s-deficient cell lines and methods for use of same for producing exogenous polypeptides, e.g., human immunodeficiency virus (HIV) envelope glycoprotein polypeptides, such as, gp120 or human Factor VIII are provided.

Provided is an isolated monoclonal antibody and its antigen-binding fragment that specifically binds to an epitope in the serine protease domain of human MASP-2. In some embodiments, the antibody or its antigen-binding fragment inhibits lectin pathway complement activation. Also provided is a polynucleotide that encodes the monoclonal antibody or its antigen-binding fragment of the present disclosure, and a cloning vector or expression cassette that includes such a polynucleotide. Further provided is a method for inhibiting lectin pathway complement activation and a method for treating diseases and disorders of the lectin pathway. TIFF2024546109000142.tif97161

Provided are a peptidyl nitrile compound and a use thereof; specifically provided are a compound represented by formula (I) and / or a pharmaceutically acceptable salt thereof, a pharmaceutical composition comprising the compound and / or the pharmaceutically acceptable salt thereof, a method for preparing the compound, and a use of the compound in treating diseases caused by cathepsin C and a downstream serine protease thereof.

The application discloses a bacillus velezensis serine protease variant and application thereof. The serine protease variant is obtained by sequentially mutating a plurality of amino acid residues in a parent serine protease amino acid sequence, and still maintains the ability of the parent serine protease to hydrolyze a peptide bond; the amino acid sequence homology of the two reaches more than 95%. The serine protease variant provided by the application has higher catalytic activity after being incubated for 4 hours under an acid condition of pH 2-5 and for 12 hours under an acid condition of pH 2.2. The serine protease mutant provided by the application has better in-vitro enzymolysis effect on piglet feed than the original protease under the conditions of pH 2.2, a temperature of 40 DEG C, different enzyme addition amounts, different enzymolysis time and different solid-liquid ratios. The serine protease mutant provided by the application has good acid resistance, heat stability and excellent feed enzymolysis effect. When the enzyme addition amount is 400 U, the enzymolysis time is 4 hours, and the solid-liquid ratio is 0.7 g / mL, the enzymolysis benefit of the mutant enzyme is higher than that of other groups.

The disclosure demonstrates the role of mast cell stabilizers in treating rosacea. The disclosure also shows the role of mast cells, cathelicidin, serine protease and / or vitamin D3 in rosacea pathology and the use of antagonists and inhibitors thereof to treat rosacea.

A serine protease derived from M. luteus. is disclosed. Also disclosed are compositions comprising the serine protease and associated uses and method of manufacture.

Antibodies against the protease 2 (MTP-2) are provided. Inhibition of MTP-2 reduces dietary iron uptake and reduces release of iron from cellular stores in the body. Inhibitors of MTP-2, such as antibodies against the serine protease domain, are useful in the treatment of iron overload, which is characteristic of diseases such as beta-thalassemia and would otherwise result in toxic accumulation of iron. Combinations of MTP-2 inhibitors with activin receptor ligand traps or with erythropoietin provide additional therapeutic effects.