23 results about "Linear epitope" patented technology

The present application relates to the field of biotechnology and in vitro diagnosis, and relates to a monoclonal antibody of eosinophil peroxidase and application thereof. The antibody of the present application is mainly used for detecting the content of eosinophil peroxidase by western blot. The monoclonal antibody of eosinophil peroxidase of the present application is prepared by immunizing Balb / c mice with recombinant eosinophil peroxidase as an immunogen, then fusing the spleen with myeloma cells NS1, and screening and purifying. The prepared monoclonal antibody of eosinophil peroxidase specifically recognizes the linear epitope of eosinophil peroxidase.

A tumor vaccine for treating esophageal squamous cell carcinoma and other cancers, and a composition thereof. Specifically, provided is a polypeptide, which contains one or more antigen fragments selected from: ACTL8, BRDT, FOXI3, GNGT1, SMC1B, PLAC1, MAGEA1, MAGEA3, MAGEA4, MAGEA6, MAGEA10 and MAGEA11, wherein the one or more antigen fragments are linked via a linker peptide, and the antigen fragments contain one or more antigenic epitope peptides. Furthermore, provided are a linear epitope peptide, a nucleic acid encoding the polypeptide and the linear epitope peptide, and the use of the polypeptide or the linear epitope peptide in the preparation of a drug for preventing or treating cancers such as esophageal squamous cell carcinoma.

This invention discloses monoclonal antibodies that recognize linear B-cell epitopes in the conserved extracellular domain of pseudorabies virus (PRV) gE protein and their applications. Using recombinant PRV gE protein extracellular domain protein as an immunogen, hybridoma cell lines were prepared. Combining dot blot and peptide scanning techniques, two monoclonal antibodies, 4E5D7 and 8F6B2, were screened to recognize the 69-93aa region of the conserved extracellular domain of the PRV gE protein. Both antibodies achieved a titer of 1:2048000 and specifically recognized the native PRV wild-type gE protein, showing no cross-reactivity with gE gene-deleted vaccines. The monoclonal antibodies of this invention fill the gap in detection reagents targeting the precise epitopes of the 69-81aa and 79-93aa extracellular domains of the PRV gE protein, thus improving the linear B-cell epitope map of the PRV gE protein. These monoclonal antibodies can be used for research on the pathogenesis of PRV and the development of specific detection reagents for PRV wild-type strains, possessing significant application value and translational prospects in basic scientific research, veterinary clinical testing, and animal disease prevention and control.

The invention provides a monoclonal antibody of a canine distemper virus and application thereof, and belongs to the technical field of animal medicine detection. The antibody provided by the invention has ultrahigh binding affinity to the CDV H protein of the canine distemper virus, and the linear epitope is the 373-381 site of the CDV H protein. According to the kit disclosed by the invention, the nitrocellulose membrane is adopted to coat the canine virus specific antibody and the fluorescent marker, so that the virus in a canine sample can be rapidly detected. The adopted antibody is prepared through a genetic engineering means, and the detection sensitivity of the antibody is obviously superior to that of a conventional colloidal gold test strip and an ELISA detection method. The antibody disclosed by the invention keeps excellent stability in a high-temperature environment, and shows an extremely low cross reaction characteristic to pathogens such as CAV. By matching with a special fluorescence detection device, the technology can complete efficient detection of the canine distemper virus in a short time, and is suitable for clinical diagnosis and treatment and on-site rapid screening scenes.

The application provides preparation and application of a diagnostic monoclonal antibody for a new epitope of human neutrophil lipocalin (HNL). Two new HNL protein conformation epitopes and one new HNL linear epitope are designed and provided, and an anti-HNL antibody with higher binding affinity and better binding specificity is screened to combine the new epitopes. The anti-HNL antibody of the application can be used for preparation of an HNL detection reagent and kit, and has higher sensitivity and specificity when used for detecting HNL protein in a sample, and can be applied to distinguishing bacterial infection and viral infection.

The invention discloses an N protein recombinant antigen for detecting a new bunyavirus antibody and application of the N protein recombinant antigen. The N protein recombinant antigen comprises an N protein and a peptide fragment containing a linear epitope in the N protein. The N protein recombinant antigen completely covers SFTSV antibody recognition sites and has high activity, and the prepared protein is high in purity, stable in structure and good in batch-to-batch stability.

The present invention relates to a method for predicting immunogenic epitopes and an apparatus using the same. The method for predicting immunogenic epitopes according to the present invention includes the steps of: calculating the degree of influence of factors involved in a biological process of a tumor cell for an epitope and characteristics of the epitope on the immunogenicity of the epitope; performing at least one of standardization and normalization on the calculated value; and inputting the value after the standardization and normalization into a pre-trained artificial intelligence model to predict the immunogenicity of the epitope. The biological process may include an antigen processing stage, an antigen presentation stage, an immune stage, and a tumor microenvironment, and the factors involved in the tumor microenvironment may be at least one of an inflammatory response, a B-cell linear epitope, and a B-cell conformational epitope.

The application discloses a monoclonal antibody of a porcine rotavirus VP6 protein, an epitope of the monoclonal antibody and application of the monoclonal antibody. The monoclonal antibody can specifically recognize a linear B cell epitope on the VP6 protein, and a core sequence of the epitope is TTRLSFQLVR. The antibody has high affinity and high specificity, and can cross-react with porcine rotaviruses of various genotypes such as G5, G9 and G11. The application further includes an indirect ELISA detection kit containing the monoclonal antibody, and application of the linear epitope in detection of porcine rotaviruses, development of vaccines and research on functions of viral proteins. The application provides an important tool and theoretical basis for serological diagnosis, vaccine evaluation and etiological research of porcine rotaviruses.

The invention relates to the technical field of riemerella anatipestifer detection, and provides a biomarker and a detection method for detecting riemerella anatipestifer, and the biomarker is a host mucosal lesion product generated by induction of specific virulence factors of riemerella anatipestifer after duck infection. Comprising a mucoprotein cracking fragment containing a linear epitope GTTPSPVP, a sialylated sugar chain containing a specific sialic acid modification motif, and a Muc2 degradation peptide fragment. The detection method comprises the following steps: collecting a sample, pretreating, detecting corresponding markers for excrement, respiratory tract lavage fluid and mucous membrane scrape samples by adopting ELISA (Enzyme-Linked Immunosorbent Assay), an immunochromatography test strip and a lectin chip respectively, and judging a result according to a set threshold value. The kit is high in specificity, covers the whole infection period, can realize early and on-site rapid detection, and improves the diagnosis reliability.

The application discloses a method for reducing the allergenicity of tenebrio molitor by ultrasonic and enzymatic hydrolysis, and relates to the technical field of food processing and food safety. First, the tenebrio molitor protein is extracted by an alkali solution method, and then the tenebrio molitor protein solution is treated by ultrasonic and enzymatic hydrolysis to change the conformational epitope and linear epitope of the tenebrio molitor protein, and finally, the treated tenebrio molitor protein solution is freeze-dried to obtain tenebrio molitor protein powder with low allergenicity. The ultrasonic cavitation effect and the specific hydrolysis of enzymatic hydrolysis are used to produce a synergistic effect, and under the combined treatment of 300 W ultrasonic power and alkaline protease, the allergenicity reduction rate can reach more than 70%, which is significantly better than single processing mode, and provides technical support for the development of tenebrio molitor low allergenic food.

The invention discloses a neutralizing monoclonal antibody aiming at a pig delta coronavirus S1 protein conserved linear epitope and application of the neutralizing monoclonal antibody, and belongs to the technical field of biology. The amino acid sequence of a light chain of the neutralizing monoclonal antibody is as shown in SEQ ID NO.9, and the amino acid sequence of a heavy chain of the neutralizing monoclonal antibody is as shown in SEQ ID NO.13. According to the invention, an insect baculovirus expression system is utilized to express the S1 protein of the porcine delta coronavirus and screen out a linear epitope with a neutralizing effect, and a neutralizing monoclonal antibody is harvested. The monoclonal antibody can be subjected to neutralization reaction with multiple strains of porcine delta coronaviruses, and is strong in neutralization activity and high in titer. The neutralizing monoclonal antibody provided by the invention can be used for efficiently preventing and treating the porcine delta coronavirus. The invention provides a new way for diagnosing, preventing and treating the porcine delta coronavirus, and provides a theoretical basis for development of related medicines and vaccines.

This invention relates to a double-antibody sandwich ELISA kit for detecting serum PTGS1 protein, comprising: a PTGS1 capture antibody, an unlabeled PTGS1 detection antibody, an enzyme-labeled IgG secondary antibody, a solid-phase carrier, an enzyme substrate, a blocking buffer, a washing buffer, and a stop solution; the IgG secondary antibody specifically binds to the PTGS1 detection antibody; the PTGS1 capture antibody is a rabbit monoclonal antibody that specifically binds to the linear epitope A of human PTGS1 protein, the amino acid sequence of which is SEQ ID NO:1, corresponding to amino acids 271-282 of human PTGS1 protein; the PTGS1 detection antibody is a mouse monoclonal antibody that specifically binds to the B epitope of human PTGS1 protein; the amino acid sequences of the B epitope at the A epitope do not overlap and do not constitute steric hindrance. This kit avoids the conserved homologous region between PTGS1 and its homologous protein PTGS2, ensuring the accuracy of the capture antibody recognition, and uses an indirect detection mode with enzyme-labeled goat anti-mouse IgG secondary antibody to achieve signal cascade amplification, significantly improving detection sensitivity.

The application provides a monoclonal antibody of canine distemper virus and application, and belongs to the animal medical detection technical field.The antibody provided by the application has super-high binding affinity to CDV H protein of the canine distemper virus, and the linear epitope is the 373-381th position of the CDV H protein.The kit of the application adopts nitrocellulose membrane to coat the canine virus specific antibody and a fluorescent marker, and can rapidly detect the virus in the canine sample.The antibody is prepared by a genetic engineering means, and the detection sensitivity is significantly better than that of a conventional colloidal gold test strip and an ELISA detection method.The antibody of the application maintains excellent stability in a high-temperature environment, and shows extremely low cross-reaction characteristics to CAV and other pathogens.Coupled with a special fluorescent detection device, the technology can complete efficient detection of the canine distemper virus in a short time, and is suitable for clinical diagnosis and treatment and on-site rapid screening scenes.

The application provides a method for identifying neutralizing antigen epitopes in bovine coronavirus spike protein, immunogens, compositions and uses, relates to the technical field of biology, and specifically constructs an efficient neutralizing epitope identification route: online prediction, nanoparticle multivalent display, animal immunization, combined evaluation of binding and neutralization, which can screen out epitopes with neutralizing activity from candidate linear epitopes in a relatively short period of time; the multivalent presentation of ferritin nanoparticles significantly improves the detectability of the immune response of weak immunogenic linear peptides; the obtained epitopes can directly serve the development of subunit vaccines, multi-epitope nanovaccines and in vitro diagnostic reagents.

The invention provides a method for identifying a neutralizing epitope of bovine coronavirus spike protein, an immunogen, a composition and application, and relates to the technical field of biology, the method specifically constructs an efficient neutralizing epitope identification route: on-line prediction, nanoparticle multivalent display, animal immunization, and combined evaluation of associativity and neutrality. Epitopes with neutralizing activity can be screened out from candidate linear epitopes in a short period; the multivalent presentation of the ferritin nanoparticles significantly improves the immune response detectability of the weak immunogenicity linear peptide fragment; the obtained epitope can be directly used for development of subunit vaccines, multi-epitope nano vaccines and in-vitro diagnostic reagents.

The application belongs to the technical field of biology and relates to a broad-spectrum monoclonal antibody for recognizing a linear antigen epitope at the C-terminal of foot-and-mouth disease virus VP2 protein and application thereof. The monoclonal antibody pOTB-1 is successfully constructed, the amino acid sequence of the heavy chain variable region is as shown in SEQ ID No. 6, and the amino acid sequence of the light chain variable region is as shown in SEQ ID No. 7. The biological activity of the antibody is verified by indirect immunofluorescence test, enzyme-linked immunosorbent assay and Western-blot. The antibody exhibits broad-spectrum reactivity to O type and A type FMDV and has strong binding affinity. The antibody recognizes a continuous linear B cell epitope at the C-terminal of the structural protein VP2. The epitope sequence is highly conserved among FMDV O type, A type and Asia1 type, which indicates that there is an inter-type common antigen site in the capsid protein VP2. A competitive ELISA detection method is established based on biotinylated pOTB-1, which provides a tool for the prevention and control of FMDV and serological detection, and lays a foundation for the design of FMDV marker vaccine and the evaluation of immunization effect.

The invention relates to a double-antibody sandwich ELISA kit for detecting serum PTGS1 protein. The double-antibody sandwich ELISA kit comprises a PTGS1 capture antibody, a non-labeled PTGS1 detection antibody, an enzyme-labeled IgG secondary antibody, a solid-phase carrier, an enzyme substrate, a confining liquid, a washing liquid and a stop solution, the IgG secondary antibody can be specifically combined with the PTGS1 detection antibody; the PTGS1 capture antibody is a rabbit monoclonal antibody specifically combined with a human PTGS1 protein A linear epitope, the amino acid sequence of the A linear epitope is SEQ ID NO: 1, and the A linear epitope corresponds to the 271th to 282th amino acids of the human PTGS1 protein; the PTGS1 detection antibody is a mouse monoclonal antibody which is specifically combined with a human PTGS1 protein B epitope; and the amino acid sequence of the B epitope at the A epitope is not overlapped and does not form steric hindrance. According to the kit, conserved homologous segments of PTGS1 and homologous protein PTGS2 are avoided, the recognition accuracy of a captured antibody is ensured, signal cascade amplification is realized by adopting an indirect detection mode of an enzyme-labeled goat anti-mouse IgG secondary antibody, and the detection sensitivity is remarkably improved.

The invention discloses a monoclonal antibody of porcine rotavirus VP6 protein, an epitope of the monoclonal antibody and application of the monoclonal antibody, the monoclonal antibody can specifically recognize linear B cell epitopes on the VP6 protein, and the epitope core sequence of the monoclonal antibody is TTRLSFQLVR. The antibody has high affinity and high specificity, and can be subjected to cross reaction with various genotypes of porcine rotaviruses such as G5, G9, G11 and the like. The invention also comprises an indirect ELISA detection kit containing the monoclonal antibody, and application of the linear epitope in porcine rotavirus detection, vaccine research and development and virus protein function research. The invention provides an important tool and theoretical basis for serological diagnosis, vaccine evaluation and etiological research of the porcine rotavirus.

The invention provides preparation and application of a monoclonal antibody for diagnosis aiming at a human neutrophil lipocalin (HNL) neoepitope. Two new HNL protein conformational epitopes and a new HNL linear epitope are designed and provided, and the anti-HNL antibody which is combined with the new epitopes and has higher binding affinity and better binding specificity is obtained through screening. The anti-HNL antibody disclosed by the invention can be used for preparing an HNL detection reagent and a kit, has higher sensitivity and specificity when being used for detecting HNL protein in a sample, and can be applied to distinguishing bacterial infection and virus infection.

The present application provides a kind of polypeptide, polypeptide composition, kit and related application.The polypeptide is the polypeptide shown in SEQ ID NO:1 to SEQ ID NO:85, can be specifically bound as follows target antibody: human SNRPC / U1C antibody, human PCNA antibody, human CENPB antibody, human NUP210 / gp210 antibody, human FTCD / 58K golgi protein antibody and GAD antibody.The above-mentioned multiple specific binding target antibody polypeptide or polypeptide set can cover the peptide segment including linear epitope and nonlinear epitope, so that the number of polypeptides used can be reasonably selected according to the number of target antibodies to be detected, which can improve the detection sensitivity and specificity of each polypeptide, improve the detection accuracy, and improve the throughput and efficiency of the detected antibody.

The application belongs to the technical field of immunology and in vitro diagnosis, and relates to a monoclonal antibody capable of specifically recognizing bluetongue virus VP5 protein. A BTV-1 recombinant VP5 protein with N-terminal 1-79 amino acids deleted is expressed; after the protein is used to immunize mice, a monoclonal antibody 5H11 against the BTV-1 VP5 protein is screened, and the heavy chain and light chain variable region sequences coding the antibody are obtained; the monoclonal antibody 5H11 can specifically react with the BTV-1 VP5 protein, and can specifically recognize the natural VP5 protein in the BTV-1 infected cells; through twice truncation expression of the BTV-1 VP5 protein, a B cell linear epitope recognized by the 5H11 on the VP5 protein is identified, which lays a foundation for in-depth study on the structure and function of the BTV VP5 protein and development of a novel vaccine.

The application discloses a type 2 GAstV capsid protein monoclonal antibody and an antigen epitope peptide thereof. The monoclonal antibody is prepared after a mouse is immunized with a type 2 goose astrovirus capsid protein GAstV Cap as an antigen and is named 1F1. The monoclonal antibody 1F1 comprises a heavy chain variable region and a light chain variable region, and the amino acid sequences are shown in SEQ ID No. 3 and SEQ ID No. 5 in sequence. In order to determine the B cell antigen epitope of the screened monoclonal antibody, a GAstV Cap truncated fusion protein is constructed, and antigen recognition epitopes are determined through indirect ELISA and Western blotting experiments, so that the monoclonal antibody is screened step by step until the shortest linear epitope recognized by the monoclonal antibody is determined, and the amino acid sequence is shown in SEQ ID No. 10. Therefore, the monoclonal antibody and the antigen epitope thereof in the application can be applied to the research on the structure and function of the GAstV capsid protein, serological diagnostic tools and the preparation of epitope vaccines.

The present application relates to a kind of B cell linear epitope identification method of sesame allergen protein Sesi3, comprising the following steps: first, the B cell linear epitope of sesame allergen Sesi3 is predicted by bioinformatics technology;Then, the B cell linear epitope of sesame allergen Sesi3 is identified by slot-blot immunomicroarray technology combined with immune score matrix.The B cell linear epitope identification method of sesame allergen protein Sesi3 of the present application has the advantages of strong specificity, high sensitivity, high accuracy and high throughput.