52 results about "Cross-reactivity" patented technology

The invention relates to a medetomidine hapten, a monoclonal antibody, a hybridoma cell strain and application thereof, and belongs to the technical field of immunodetection. A medetomidine complete antigen is obtained by synthesizing a medetomidine hapten, a mouse is used as an immune animal to prepare a hybridoma cell strain secreting a medetomidine monoclonal antibody, the hybridoma cell strain is preserved in the China General Microbiological Culture Collection Center (CGMCC), and the preservation number is CGMCC NO.46518. The medetomidine monoclonal antibody secreted by the hybridoma cell strain has better detection sensitivity and detection specificity to medetomidine, the IC50 value is 10.42 ng / mL, and the cross reaction rate to various medetomidine analogues is lt; the method can be applied to preparation of medetomidine detection products, and provides a reliable tool for immunodetection of medetomidine.

The application belongs to the technical field of biology and particularly relates to an ELISA kit for detecting chicken astrovirus type II antibodies and a preparation method. The Cell-ELISA experiment is carried out by using LMH cells infected with chicken astrovirus type II to detect the chicken astrovirus type II antibodies. The method has no cross reactivity with positive serum of Newcastle disease virus, avian influenza virus, chicken infectious anemia virus, avian leukosis virus, Marek's virus and chicken infectious bursal virus, which indicates that the method has good specificity. The Cell-ELISA method is used to detect the chicken serum sample to be detected by using whole virus infection, and is assembled into a kit for measuring chicken astrovirus antibodies in serum. The kit can be used for serological diagnosis of chicken astrovirus type II infection, monitoring of the level of antibodies, epidemiological investigation and the like, and provides a novel and effective detection means for prevention and treatment of chicken astrovirus type II.

The invention provides a fish creatine kinase sensitization and immune cross reactivity analysis method which comprises the following steps: preparing a fish muscle water-soluble protein crude extract, separating 40-45kDa protein components in the fish muscle crude extract through SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis), and screening a target sensitization protein combined with IgE / IgG through immunoblotting; the method comprises the following steps: extracting total RNA of grass carp and synthesizing cDNA, designing a creatine kinase specific primer for amplification to obtain a creatine kinase gene sequence, and carrying out bioinformatics analysis after sequencing verification; the method comprises the following steps: cloning a creatine kinase gene to an expression vector, transforming escherichia coli BL21, performing IPTG induced expression, and performing urea gradient dialysis renaturation on an inclusion body to obtain the recombinant grass carp creatine kinase. Detecting the IgE binding activity of the recombinant grass carp creatine kinase and the serum of the allergic patient through dot hybridization; the IgG cross reactivity of the recombinant grass carp creatine kinase and the blue crab arginine kinase is verified through indirect ELISA; the IgE cross reaction degree of the recombined grass carp creatine kinase and the blue crab arginine kinase is quantified through inhibitory dot hybridization.

The invention discloses an antigen binding fragment of an anti-human PRAME protein, a monoclonal antibody as well as preparation and application of the monoclonal antibody. CDR1 of a heavy chain variable region of the antigen binding fragment of the anti-human PRAME protein comprises an amino acid sequence as shown in SEQ ID NO.1, CDR2 comprises an amino acid sequence as shown in SEQ ID NO.2, and CDR3 comprises an amino acid sequence as shown in SEQ ID NO.3; cDR1 of a light chain variable region of the antigen binding fragment of the anti-human PRAME protein comprises an amino acid sequence as shown in SEQ ID NO.4, CDR2 of the light chain variable region of the antigen binding fragment of the anti-human PRAME protein comprises an amino acid sequence as shown in SEQ ID NO.5, and CDR3 of the light chain variable region of the antigen binding fragment of the anti-human PRAME protein comprises an amino acid sequence as shown in SEQ ID NO.6. The monoclonal antibody provided by the invention has high specificity and low cross reactivity, can efficiently and specifically recognize natural and denatured PRAME proteins, and is suitable for immunological detection, especially immunohistochemical detection.

Provided herein are recombinant T-cell receptors (TCRs) that can selectively recognize the MAGE-A4-derived peptide GVYDGEEHSV or KVEEHVVRV when presented by HLA-A*0201 sufficiently to activate the recombinant T cell. TCRs provided herein were thoroughly screened for lack of cross-reactivity with similar peptides that may be presented by normal cells or tissue and for alloreactivity.

The present invention relates to humanized anti-Lewis Y antibodies that specifically bind Lewis Y and do not show any cross-reactivity. In particular, the humanized anti-Lewis Y antibodies do not bind to Lewis b or any other blood group carbohydrate antigen. In particular, the present invention relates to humanized anti-Lewis Y antibodies for use in the treatment of cancer.

The present application relates to a hybridoma cell strain secreting clozapine and its metabolite monoclonal antibody, and belongs to the technical field of immune detection. The present application prepares a hapten by chemically synthesizing clozapine and its metabolite, and then prepares a complete antigen, and then screens a hybridoma cell strain secreting clozapine and its metabolite monoclonal antibody through animal immunization and cell fusion. The hybridoma cell strain LDP-2B10 provided by the present application has been preserved in the China General Microbiological Culture Collection Center (CGMCC) with a preservation number of CGMCC No. 46233. The monoclonal antibody secreted by the hybridoma cell strain has good sensitivity and specificity, the IC 50 value of the monoclonal antibody for clozapine is 5.041 ng / mL, the IC 50 value of the monoclonal antibody for the metabolite N-desmethylclozapine is 5.524 ng / mL, and the IC 50 value of the monoclonal antibody for the metabolite clozapine-N-oxide is 5.551 ng / mL. The cross reactivity of the monoclonal antibody for various clozapine functional analogues is less than 1%, and the monoclonal antibody can be used for detecting clozapine in urine and blood drug concentration, and has practical application value.

The invention belongs to the technical field of antibody preparation, and particularly relates to an anti-MLH1 protein monoclonal antibody and application thereof in immunodetection. Amino acid sequences of CDR1-3 on a light chain variable region of the antibody are respectively shown as SEQ ID NO.3-5, and amino acid sequences of CDR1-3 on a heavy chain variable region of the antibody are respectively shown as SEQ ID NO.8-10. The antibody provided by the invention has strong specificity, high recognition sensitivity and good binding affinity for human MLH1 protein in cells and tissues, can accurately recognize and locate target protein in cells and tissues, greatly reduces the occurrence rate of false positive and false negative results, and can be applied to a plurality of immunodetection systems, such as human MLH1 protein, human MLH1 protein, human MLH1 protein, human MLH1 protein, human MLH1 protein and human MLH1 protein. Particularly, the method has good applicability in immunoblotting and immunohistochemical systems. Moreover, the antibody provided by the invention has cross reactivity to human and mouse homologous MLH1 proteins, and also has certain applicability and good application prospects in detection of mouse MLH1 proteins.

The application discloses a CD3 antibody and application thereof, and relates to the technical field of biological medicine.The antibody provided by the application is a full human antibody, which fundamentally reduces immunogenicity risk, and lays a material foundation for developing safer T cell redirection therapy.The antibody has cross-reactivity with cynomolgus monkey CD3, can be directly used for a cynomolgus monkey model to perform systematic pharmacodynamics, pharmacokinetics and safety evaluation, greatly improves the prediction value of preclinical data, and accelerates the conversion process of a candidate molecule to clinical research.

This invention provides novel allergy antigens that are proteins. It also provides polypeptide antigens containing epitopes. [Solution] A novel antigen of a protein to which IgE antibodies in the serum of patients with wheat allergy specifically bind. Furthermore, since the epitope has a relatively short amino acid sequence, if the same amino acid sequence exists in different allergen components, the IgE antibody can bind to multiple allergen components. As a result of the existence of a common epitope in different allergen components, the IgE antibodies of allergic patients bind to both, and the antigen exhibits cross-reactivity.

This invention is directed to a monoclonal antibody or an antigen binding fragment thereof targeting the expression and function of CYP1A1 with cross reactivity across the vertebrate taxa. This invention is also directed to nucleic acid molecules, vectors, host cells and compositions comprising the same, as well as methods for use of the same and for producing the same.

The invention discloses a monoclonal antibody LayG-1069 of a Langya virus G protein as well as preparation and application of the monoclonal antibody LayG-1069. The monoclonal antibody LayG-1069 for the Langya virus G protein, which is obtained by screening, is high in binding capacity with the LayV G protein, and is relatively high in cross reactivity with the MojV G protein. The application of the monoclonal antibody LayG-1069 in various biological methods is verified through the embodiment of the invention, and the monoclonal antibody LayG-1069 has ADCC and ADCP activities. The monoclonal antibody LayG-1069 is expected to become a detection antibody for LayV and MojV infection, and has the potential of becoming a candidate drug for treating LayV and MojV infection.

The invention provides a PRLR monoclonal antibody with human-monkey cross reactivity and application of the PRLR monoclonal antibody. Specifically, the invention provides an antibody targeting PRLR or an antigen binding fragment thereof, and a heavy chain variable region of the antibody comprises the following complementarity determining regions CDR: VHCDR1-3 as shown in SEQ ID NO: 6-8; the light chain variable region comprises the following complementarity determining regions CDR: VLCDR1 to VLCDR3 as shown in SEQ ID NO: 2 to SEQ ID NO: 4. The antibody provided by the invention can specifically recognize and bind to PRLR protein, can mediate internalization after binding to the PRLR protein expressed on the cell surface, and can bind to human and monkey PRLR antigens and inhibit the growth and / or proliferation of tumors or tumor cells.

To provide a method for improving cross-reactivity, that is, improving specificity in an immunoassay method using anti-immunocomplex antibody.SOLUTION: A method of immunoassay includes the following steps (i) to (iii): (i) reacting an anti-hapten rabbit monoclonal antibody indirectly immobilized on a water-insoluble carrier with a hapten (for example, digoxin) in a solution to be measured; (ii) reacting a labeled anti-immunocomplex mouse monoclonal antibody with a hapten-anti-hapten antibody immune complex; and (iii) detecting a signal derived from the label.SELECTED DRAWING: Figure 2

The invention relates to the technical field of poultry immunology, in particular to a universal riemerella anatipestifer monoclonal antibody, a detection kit and application of the universal riemerella anatipestifer monoclonal antibody. Specifically, the invention successfully designs the universal riemerella anatipestifer monoclonal antibody, and the detection kit developed based on the monoclonal antibody can rapidly detect the level of the riemerella anatipestifer serum antibody in a sample, and has high sensitivity and strong specificity. The riemerella anatipestifer strain has no cross reactivity with avian enterococcus faecalis, avian salmonella typhimurium, avian escherichia coli and avian salmonella enteritidis, so that the riemerella anatipestifer strain can be applied to rapid screening, epidemiological monitoring and vaccine immune effect evaluation of riemerella anatipestifer infection, and has a wide application prospect.

The application relates to the technical field of rapid detection methods, in particular to a rapid detection method of proteus mirabilis which is not for disease diagnosis or treatment purposes, first, the RPA reaction system and the CRISPR / Cas12a reaction system are respectively placed at the bottom of a PCR reaction tube and the inner side of the tube cover, so that the competition between CRISPR / Cas12a and RPA is avoided, the reaction rate and sensitivity are ensured, and because the tube cover does not need to be opened, the risk of nucleic acid aerosol pollution is also avoided; second, the RPA provided by the application specifically amplifies target DNA through preferred primers, the CRISPR / Cas12a specifically recognizes a target sequence through preferred crRNA, and under preferred reaction conditions, through the double screening of the RPA and the CRISPR / Cas12a, the proteus mirabilis can be rapidly, sensitively and specifically detected, the reliability is high, the cross reactivity is low, and the application is convenient to popularize.

Described herein are multiplex single molecule assays for ultrasensitive detection of biomolecules, based on an ultrasensitive multiplex digital ELISA platform that substantially reduces cross-reactivity, and methods of use thereof.

The invention relates to the technical field of biochemical engineering, in particular to fipronil hapten and a preparation method thereof, artificial antigen, monoclonal antibody and application. The hapten has a chemical structure as shown in a formula I or a formula II. The invention also relates to an artificial antigen obtained by connecting the hapten and a carrier protein. The application comprises the following steps: (1) preparing a specific antibody for resisting fipronil or main metabolites thereof; (2) detecting a specific antibody resisting fipronil or main metabolites thereof; and (3) preparing a reagent for detecting a specific antibody resisting fipronil or main metabolites thereof. The hapten provided by the invention can expose common epitopes of fipronil and metabolites thereof to the greatest extent, can be used for preparing broad-spectrum specific monoclonal antibodies with uniform cross reaction rate and high sensitivity, and can realize high-specificity and sensitivity detection of fipronil or main metabolites thereof.

The invention relates to a diafenthiuron hapten, a monoclonal antibody, a hybridoma cell strain and application thereof, and belongs to the technical field of immunodetection. A diafenthiuron hapten is synthesized, then the diafenthiuron hapten is coupled with protein to obtain a diafenthiuron complete antigen, a hybridoma cell strain secreting the diafenthiuron monoclonal antibody is obtained through the steps of mouse immunization, cell fusion and the like, the hybridoma cell strain is preserved in the China General Microbiological Culture Collection Center (CGMCC), and the preservation number is CGMCC NO.46519. The monoclonal antibody provided by the invention has high sensitivity and high specificity to diafenthiuron, the IC50 value is 1.18 ng / mL, and the cross reaction rate to various diafenthiuron analogues is 1t; the method can be applied to preparation of diafenthiuron detection products, and an efficient tool is provided for diafenthiuron immunodetection.

The invention provides a molecularly imprinted polymer for specifically recognizing human IgG as well as a preparation method and application of the molecularly imprinted polymer, and relates to the technical field of affinity purification and biological pharmacy quality control. According to the method, chemically modified C-terminal polypeptide of human IgG1 is used as a characteristic epitope, an imprinting cavity with a specific recognition epitope is constructed on the surface of a functionalized substrate through a molecular imprinting technology, and a coating layer is introduced into a non-imprinting area to reduce non-specific adsorption, so that the molecularly imprinted polymer capable of specifically recognizing human IgG is obtained. The molecularly imprinted polymer prepared by the preparation method has high affinity (dissociation equilibrium constants reach 10 <-9 > M) and selectivity (cross reactivity to other proteins is less than or equal to 9.1%; the cross reactivity to IgG from other sources is less than or equal to 19.7%, which is superior to industrial'gold standard 'protein A and protein G for IgG purification, has good stability, can be stored and recycled for a long time, and can be prepared into various material forms to adapt to different application scenes.

The present application relates to a kind of bifenthrin secreting monoclonal antibody hybridoma cell strain and its application, belong to immune detection technical field.The present application is prepared by screening and obtains a kind of bifenthrin secreting monoclonal antibody hybridoma cell strain, the monoclonal antibody of hybridoma cell strain of the present application has good sensitivity and specificity to bifenthrin, specifically, the IC 50 Value of the monoclonal antibody of the present application to bifenthrin is 1.84 ng / mL, and the cross reactivity of bifenthrin analog (imidacloprid, buprofezin, pymetrozine, chlorbenzuron, diflubenzuron, metalaxyl) is less than 10%, so low concentration bifenthrin can be accurately detected.

The invention discloses an anti-histone antibody, an anti-histone antibody immunodetection quality control product as well as a preparation method and application of the anti-histone antibody immunodetection quality control product. The anti-histone antibody comprises a heavy chain variable region and a light chain variable region, the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 of which the amino acid sequences are respectively shown as SEQ ID NO: 4-6, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 of which the amino acid sequences are respectively shown as SEQ ID NO: 1-3. The anti-histone antibody has high specificity and low cross reactivity, and low-cost large-scale preparation can be realized. The quality control product based on the antibody has the advantages of excellent stability, high recovery rate and low matrix effect through formula and process optimization, is highly consistent with clinical serum, and significantly improves the detection reliability.

The invention relates to antibody compositions for reducing cross reactivity between antibodies specific to related antigens, methods using such compositions and kits comprising such compositions.

The invention belongs to the technical field of biological medicines, and relates to a monoclonal antibody capable of being specifically combined with PD-L1 as well as a preparation method and application of the monoclonal antibody. The monoclonal antibody capable of being specifically bound with the human PD-L1 has the human PD-L1 binding activity equivalent to that of an existing anti-human PD-L1 antibody, has cross reactivity with cynomolgus monkey PD-L1 and is novel in sequence.

The application discloses a fengycin mimotope peptide which can be specifically combined with fengycin antibody, and a sensitive and rapid competitive enzyme-linked immunoassay method can be established by using the phage displaying the mimotope peptide or the mimotope peptide. 50 The IC50 is 0.30 ng / mL, and the LOD is 0.02 ng / mL, and the sensitivity of the method is improved by 60 times compared with the sensitivity of a traditional enzyme-linked immunoassay method based on a hapten; the competitive immunoassay method based on the mimotope peptide has good cross reactivity to other common structural analogues.

A region of the Trichomonas vaginalis AP65-1 gene has been identified which is useful for performing amplification assays to determine specifically whether T. vaginalis is present in the sample being tested. Oligonucleotides useful for performing thermal Strand Displacement Assay (tSDA) reactions on this gene are disclosed. The disclosed oligonucleotides can be used in an assay which is specific for multiple strains of T. vaginalis and which does not show cross reactivity with the genomes of other microorganisms or with human DNA.

The application belongs to the technical field of biology and relates to an anti-OX40L nanobody and application thereof. The anti-OX40L nanobody comprises a heavy chain variable region, the amino acid sequence of which is shown as SEQ ID NO:1, and the amino acid sequences of the complementarity determining regions CDR1, CDR2 and CDR3 thereof are shown as SEQ ID NO:3, SEQ ID NO:4 and SEQ ID NO:5 respectively. The application obtains the nanobody targeting OX40L from a llama nanobody natural library through phage display technology, does not need animal immunization, and the obtained antibody can specifically recognize Human OX40L recombinant protein, HEK293 hOX40L overexpression cells and CHO-K1 cynoOX40L overexpression cells, and exhibits good species cross-reactivity and binding activity. Based on the blocking potential of the nanobody on the OX40 / OX40L signal pathway, the nanobody shows a broad prospect in treating inflammatory and autoimmune diseases.

The present invention relates to a monoclonal antibody mutant for T4 detection and a coding nucleic acid molecule thereof, the monoclonal antibody mutant comprises complementary determining regions CDR-VL1, CDR-VL2 and CDR-VL3, the CDR-VL1 is represented by QNIYSN, the CDR-VL2 is represented by RAS, and the fifth amino acid Y, represented by QSYYYASGSTYANA, of the CDR-VL3 is deleted or substituted by a non-Y amino acid residue. According to the monoclonal antibody mutant, the cross reactivity with a free anti-T4 antibody is remarkably reduced while high-affinity binding of the monoclonal antibody mutant to a T4-T4 antibody compound is maintained. When the kit is used for T4 detection, a target immune complex and a free antibody component can be clearly and accurately distinguished in a complex clinical sample, and the kit has important clinical application value.