8 results about "C protein" patented technology

The invention discloses a colorimetric detection method for cMyBP-C protein based on nano-enzyme activity, preparation of a bismuth selenide / nano-gold composite material and application of the bismuth selenide / nano-gold composite material in protein detection. The method comprises the following steps: performing ultrasonic stripping on a bismuth selenide block to obtain a few-layer bismuth selenide dispersion liquid; and then sequentially adding a sodium borohydride aqueous solution and a chloroauric acid aqueous solution under a stirring condition, and carrying out in-situ reduction to form gold nanoparticles loaded on the surface of bismuth selenide. The composite material has the capability of catalyzing reduction of p-nitrophenol into p-aminophenol, and the color of the solution is changed from yellow to colorless. After the cMyBP-C antibody is modified on the surface of the composite material, the catalytic activity is inhibited; after a to-be-detected sample is added, the antibody and the protein are specifically combined to cause dissociation, and the catalytic activity is recovered. The cMyBP-C protein is quantitatively detected by observing the color change of the solution or monitoring the reduction of the ultraviolet absorbance at 400 nm.

The present invention discloses a monoclonal antibody capable of recognizing a novel duck reovirus NDRVσC protein, a preparation method and an application thereof, wherein the monoclonal antibody comprises a heavy chain variable region and a light chain variable region; the heavy chain variable region comprises a V sequence as shown in SEQ ID NOs: 3, 4, and 5. H CDR1, V H CDR2 and V H CDR3, the light chain variable region includes the amino acid sequences shown in SEQ ID NOs: 6, 7, and 8. L CDR1, V L CDR2 and V L CDR3. The present invention also discloses a method for preparing a monoclonal antibody and a double-antibody sandwich ELISA method based on the antibody and the σC rabbit polyclonal antibody. This method can be used to quantify NDRV subunit vaccine antigens and determine animal immunization doses. Compared with the methods reported in the literature, this ELISA method is simpler to operate and has great potential for practical application. The present invention provides a new method for evaluating NDRV immune efficacy and controlling vaccine quality, which can ensure the upgrading of NDRV vaccines.

The application discloses an antibody for detecting a novel duck reovirus (NDRV), and relates to the field of animal disease prevention and treatment.The antibody comprises a heavy chain and a light chain, wherein the amino acid sequence of the heavy chain is shown as SEQ ID NO.2, and the amino acid sequence of the light chain is shown as SEQ ID NO.4.The novel duck reovirus sigma C protein antibody can be used for directly and rapidly detecting the NDRV sigma C protein in a quick, sensitive and accurate manner when the novel duck reovirus is detected.The antibody can be used for early diagnosis of the NDRV, epidemiological investigation, and antibody screening in vaccine development, and provides an effective tool for preventing and controlling the novel duck reovirus infection.

The application belongs to the field of genetic engineering, and particularly relates to a polynucleotide construct capable of expressing LMNA and application thereof in preventing and treating DCM. The synthetic intron in the application comprises: I) a nucleotide sequence as shown in SEQ ID No. 8, II) a nucleotide sequence having at least one mutation in the 1-8th position of the sequence shown in SEQ ID No. 8, or a nucleotide sequence having at least 90% homology with the sequence shown in I) or II). By using the synthetic intron in the application, two proteins can be simultaneously expressed through alternative splicing, and the ratio of the two proteins or the expression of a single protein can be regulated through mutation of the splicing signal. Compared with the existing gene therapy method for dilated cardiomyopathy caused by LMNA mutation, the expression vector for simultaneously expressing Lamin A and Lamin C proteins in the application has stronger rescue effect.

This invention discloses a recombinant factor C protein protectant and its application. Based on the final concentration of each component, the recombinant factor C protein protectant comprises the following components: 0.05-0.2% (w / v) ProClin 300, 100-300 mM sodium chloride, 1-10 mg / mL bovine serum albumin, 5-20% (w / v) trehalose, 10-50% (v / v) glycerol, 0.1-0.5% (w / v) Tween-20, and 0.1-1 mM pH 8.0 ethylene glycol diethyl ether diaminetetraacetic acid. This invention also discloses the application of the recombinant factor C protein protectant in the cold storage of recombinant factor C protein. The recombinant C factor protein protectant and the recombinant C factor protein are mixed to prevent the recombinant C factor protein from being affected by conditions such as aggregation, oxidation, freeze-thaw cycles, and metal ion-dependent inactivation, thereby improving the stability of the recombinant C factor protein during cold storage. This ensures that the recombinant C factor protein retains ≥90% of its activity after 12 months of cold storage, and maintains its accuracy and sensitivity in detecting endotoxins.

The invention relates to the technical field of biological detection, and particularly discloses a fusion protein and application thereof in preparation of a phosphatidic acid biosensor. The fusion protein comprises circulating arrangement fluorescent protein, Nir1-N protein located at the N end of the circulating arrangement fluorescent protein and Nir1-C protein located at the C end of the circulating arrangement fluorescent protein. The amino acid sequence of the Nir1-N protein is as shown in SEQ ID NO. 1, and the amino acid sequence of the Nir1-C protein is as shown in SEQ ID NO. 2; the cyclically arranged fluorescent protein is selected from cyclically arranged green fluorescent protein, cyclically arranged yellow fluorescent protein, cyclically arranged Venus fluorescent protein and cyclically arranged blue fluorescent protein. The Nir1-N and the Nir1-C in the fusion protein can be combined with phosphatidic acid, and when the phosphatidic acid is combined with the Nir1-N and the Nir1-C, the fluorescent protein is circularly arranged to generate conformational change, so that a fluorescence signal is changed, and detection is realized.

The present disclosure addresses the problem of providing a method capable of detecting endotoxin. In addition, the present disclosure also addresses the problem of providing an endotoxin detection reagent having thermal stability. The present disclosure provides a recombinant Factor C protein having a prescribed amino acid sequence, a polynucleotide encoding the same, an endotoxin detection reagent comprising the same, and methods for producing the same. Also provided are: a recombinant Factor C protein having a prescribed amino acid substitution; a polynucleotide encoding the same; an endotoxin detection reagent comprising the same; and methods for producing the recombinant Factor C protein and the polynucleotide.

The application discloses an RNA-responsive controllable cell pyroptosis system based on a III-E type CRISPR framework and application thereof, and relates to the technical field of biology. The RNA-responsive controllable cell pyroptosis system comprises an endonuclease Cas7-11, a protease Csx29, an effector protein and crRNA; the crRNA is used for specifically recognizing target RNA; the effector protein comprises GSDMs-N protein, a linker protein and GSDMs-C protein; the linker protein is cut by the protease Csx29; the linker protein is cut by the protease Csx29; the linker protein is a Csx30 protein with an amino acid sequence as shown in SEQ ID NO. 3; or is a truncated protein obtained by truncating the Csx30 protein. The application discloses a system capable of specifically responding to target RNA and inducing target cell pyroptosis, and corresponding mRNA and effector protein, and can be widely applied to different RNA differential disease treatments. The application lays a foundation for the treatment of RNA differential diseases and provides an important technical basis for promoting the application of the DAMAGE system in the clinic.