115 results about "Cross-reactivity" patented technology

The invention provides the GPRC5D single domain and the humanized antibody thereof, the GPRC5D single domain and the humanized antibody thereof have relatively strong binding activity and reaction specificity, also have good species cross reactivity, are of great significance in research and development in different species models, and are beneficial to acceleration of a transformation process from a laboratory to clinic. The antibody sequence provided by the invention can be used for constructing CAR-T, and can be used for treating multiple myeloma.

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 invention discloses a porcine delta-coronavirus double-antibody sandwich ELISA (enzyme-linked immuno sorbent assay) detection kit based on an S protein monoclonal antibody as well as a use method and application of the porcine delta-coronavirus double-antibody sandwich ELISA detection kit. A PDCoV S protein is expressed by adopting an ExpiCHO expression system, then the purified S protein is used as an immunogen to immunize a mouse, and the monoclonal antibody is obtained. And then, respectively using the monoclonal antibody 3D7 and the MAb 9G4 labeled by the HRP as capture and detection antibodies, and establishing the double-antibody sandwich ELISA kit. The kit has good sensitivity, the detection limit of purified S protein is 0.12 ng / mL, and the detection limit of PDCoV is 1.96 * 10 < 3 > copies / [mu] L. Specificity analysis shows that the kit has no cross reactivity with other porcine intestinal coronaviruses PEDV, TGEV and PoRV with clinical symptoms similar to PDCoV, the consistency with an RT-PCR (reverse transcription-polymerase chain reaction) method reaches 91.03%, and the Kappa value is 0.814, so that the reliability of the kit for clinical sample detection is shown. In addition, the kit can also quantitatively evaluate the content of S protein in PDCoV inactivated vaccines and subunit vaccines, and provides a powerful tool for evaluating the vaccines.

The invention discloses an anti-human MMP-9 antibody and a detection kit thereof. The antibody comprises a heavy chain variable region and a light chain variable region, amino acid sequences of antigen complementary determining regions CDR1, CDR2 and CDR3 of the heavy chain variable region are respectively shown as SEQ ID NO: 3, SEQ ID NO: 4 and SEQ ID NO: 5, and amino acid sequences of antigen complementary determining regions CDR1, CDR2 and CDR3 of the light chain variable region are respectively shown as SEQ ID NO: 7, SEQ ID NO: 8 and SEQ ID NO: 9. In addition, the invention also discloses a detection kit containing the antibody, and the kit has excellent cross reactivity resistance during MMP-9 detection, and the positive-negative coincidence rate of the detection result is good.

Provided are a recombinant cat allergen, a pharmaceutical composition therefor, a preparation method therefor, and a use thereof. Compared with naturally extracted allergen products, the recombinant cat allergen has multiple advantages in desensitization immunotherapy and allergen diagnosis for cat allergic diseases. For example, high purity and high uniformity are achieved; a pure protein / peptide having specified properties and quality is defined; the allergenicity, immunogenicity, and tolerability of the allergen are predetermined; production is performed according to GMP standards; the production of a specified quantity and concentration in a reproducible manner is enabled; product standardization and quality controllability are achieved; regulatory requirements for modern pharmaceuticals and vaccines are met; and when used for diagnosis, the allergen can identify allergen molecules that truly cause allergic reactions and reveal cross-reactivity, and when used for treatment, the allergen enables targeted allergen immunotherapy for a patient, avoiding the influence of non-allergenic substances in an extract, improving the safety, and facilitating precise diagnosis, precise administration, etc.

The invention discloses a measurement method based on an antibody binding rate, and particularly relates to the field of antibody drug development and immunodetection in biopharmacy, and the method comprises the steps of antigen fixation, antibody dilution, antibody binding rate measurement and specificity index calculation. According to the scheme, the cross reactivity of the antibody is measured based on the antibody binding rate, quantification of the binding strength of the antibody and different antigens is achieved, and compared with a traditional static method, dynamic quantitative analysis of the binding rate more comprehensively evaluates the specificity and the cross reactivity of the antibody, and the detection accuracy is improved. And a more reliable analysis result is provided for antibody drug development and immunodetection.

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 present invention generally relates to an isolated arginine deiminase (ADI) protein that has reduced cross-reactivity with an anti-ADI-PEG 20 antibody compared to ADI-PEG 20, but may have functional characteristics similar to or superior to those of ADI-PEG 20; compositions comprising the ADI protein, and related methods for treating arginine-dependent diseases or related diseases such as cancer.

Provided are antibodies that specifically bind to human urokinase-type plasminogen activator receptor (uPAR). In some cases, the antibodies are cross-reactive with one or more non-human animal uPAR polypeptides, such as non-human primate uPAR, e.g., cynomolgus monkey uPAR. Fusion proteins and conjugates comprising the antibodies of the present disclosure are also provided. Methods of using the antibodies, fusion proteins, and conjugates of the present disclosure to treat conditions associated with uPAR expression and / or activity are also provided. In some embodiments, the condition associated with uPAR expression and / or activity is cancer. Non-limiting examples of such cancers include cancers characterized by cancer cells expressing uPAR on their surface, cancers characterized by stromal cells within the tumor microenvironment expressing uPAR on their surface, and the like.

To provide cross-species anti-latent TGF-β 1 antibodies which inhibit a protease mediated activation of latent TGF-β 1 without inhibiting integrin mediated activation of latent TGF-β 1.SOLUTION: To obtain the anti-latent TGF-β 1 antibodies of the present invention, anti-latent TGF-β 1 antibodies which inhibit a protease mediated activation of latent TGF-β 1 without inhibiting integrin mediated activation of latent TGF-β 1 are screened, and then humanized, and further optimized. The invention also provides combination therapies comprising an anti-latent TGF-β 1 antibody and one or more immune checkpoint inhibitors, preferably PD-1 axis binding antagonists.SELECTED DRAWING: None

The present invention belongs to the field of antibody technology, and in particular relates to monoclonal antibodies, antibody conjugates and applications thereof against p21 proteins. The amino acid sequences of the complementary determining regions CDR1-3 on the light chain variable region of the monoclonal antibody are shown as SEQ ID NO.3-5, respectively; the amino acid sequences of the complementary determining regions CDR1-3 on the heavy chain variable region are shown as SEQ ID NO.8-10, respectively. The monoclonal antibody provided by the present invention can specifically recognize p21 proteins expressed by human cells and tissues, has good affinity for binding to p21 proteins, high recognition sensitivity, and strong anti-interference ability, is suitable for immunodiagnostic analysis of p21 proteins in tissues / cells, and has broad application prospects and good market prospects in clinical diagnosis and scientific research detection. In addition, the antibody has cross-reactivity to homologous p21 proteins of humans, rats and mice, and has certain applicability to the detection of rat and mouse p21 proteins.

The integrin family of cell adhesion molecules has emerged as key mediators of tissue fibrosis. A pharmacological inhibitor of multiple integrin subtypes is required to produce meaningful effects on delaying or inhibiting the progression of fibrosis. Monoclonal antibodies recognizing multiple integrins with potent neutralizing activity and having human and mouse cross-reactivity are described. In particular, monoclonal antibodies that bind human αvβ1, αvβ3, αvβ5, αvβ36, αvβ38, and α5β1 integrins and mouse αvβ1, αvβ3, αvβ5, αvβ6, and αvβ8 integrins are described.

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 T cell receptors (TCRs) that, when recombinantly expressed on the T cell surface, can sufficiently recognize the DCAF4L2-derived peptide ILQDGQFLV (SEQ ID NO: 1) when presented by HLA-A*02:01 to activate recombinant T cells. Importantly, the exemplary TCRs provided herein have been thoroughly screened for lack of cross-reactivity with similar peptides that may be presented by normal cells or tissues, and for alloreactivity.

The present invention relates to a monoclonal antibody, a detection reagent and an application thereof for detecting human metapneumovirus. The monoclonal antibody or an antigen-binding fragment thereof of the present invention can specifically bind to the N protein of human metapneumovirus with high affinity, has a broad spectrum of effectiveness against various genotypes, and has no cross-reactivity with other respiratory viruses. Therefore, it has great potential application value in clinical detection of human metapneumovirus infection.

The present invention discloses a porcine delta-coronavirus double-antibody sandwich ELISA detection kit based on S protein monoclonal antibody, its use method and application. The PDCoV S protein was expressed using the ExpiCHO expression system, and then the purified S protein was used as an immunogen to immunize mice to obtain monoclonal antibodies. Then, a double-antibody sandwich ELISA kit was established using monoclonal antibody 3D7 and HRP-labeled MAb 9G4 as capture and detection antibodies, respectively. The kit has good sensitivity, with a detection limit of 0.12 ng / mL for purified S protein and a detection limit of 1.96×103 copies / μL for PDCoV. Specificity analysis showed that the kit had no cross-reactivity with other porcine enteric coronaviruses PEDV, TGEV and PoRV that are similar to PDCoV in clinical symptoms, and the consistency with the RT-PCR method reached 91.03%, with a Kappa value of 0.814, indicating the reliability of the kit for clinical sample detection. In addition, the kit can also quantitatively evaluate the content of S protein in PDCoV inactivated vaccine and subunit vaccine, providing a powerful tool for evaluating these vaccines.

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 application relates to a hybridoma cell strain secreting benzyl chlorophenol monoclonal antibody and its application, and belongs to the technical field of immune detection. The present application synthesizes benzyl chlorophenol hapten, prepares benzyl chlorophenol complete antigen, and through the steps of mouse immune response and cell fusion, a hybridoma cell strain secreting benzyl chlorophenol monoclonal antibody is screened and named CBP-3D4, which is preserved in the China General Microbiological Culture Collection Center with a preservation number of CGMCC NO.46222. The monoclonal antibody secreted by the hybridoma cell strain has good sensitivity and specificity, the IC 50 value of the monoclonal antibody secreted by the hybridoma cell strain for benzyl chlorophenol is 97.741 ng / mL, the cross reactivity of the monoclonal antibody for various benzyl chlorophenol functional analogs is less than 1%, and the monoclonal antibody can be applied to the preparation of benzyl chlorophenol detection products to realize the rapid quantification of benzyl chlorophenol.

The invention belongs to the technical field of antibody preparation, and particularly relates to an anti-Ki-67 protein monoclonal antibody and application thereof. Amino acid sequences of complementary determining regions CDR1-3 on a light chain variable region of the monoclonal antibody are respectively shown as SEQ ID NO.3-5; and the amino acid sequences of the complementary determining regions CDR1-3 on the heavy chain variable region are respectively shown as SEQ ID NO.8-10. The monoclonal antibody provided by the invention can effectively recognize Ki-67 protein expressed by cells / tissues, has good antigen binding specificity, relatively high affinity and excellent anti-interference capability, and is beneficial to greatly improving the accuracy, sensitivity and credibility of detecting whether the tissues / cells express Ki-67 or not; and the antibody has cross reactivity to homologous Ki-67 of human and mice (including rats and mice), and has wide detection applicability to different species of Ki-67 proteins.

The present invention discloses an antibody against human MMP-9 and a detection kit thereof. The antibody comprises a heavy chain variable region and a light chain variable region. The amino acid sequences of the antigen complementarity determining regions CDR1, CDR2 and CDR3 of the heavy chain variable region are shown in SEQ ID NO:3, SEQ ID NO:4 and SEQ ID NO:5 respectively, and the amino acid sequences of the antigen complementarity determining regions CDR1, CDR2 and CDR3 of the light chain variable region are shown in SEQ ID NO:7, SEQ ID NO:8 and SEQ ID NO:9 respectively. In addition, the present invention also discloses a detection kit comprising the antibody. The kit has excellent anti-cross-reactivity when performing MMP-9 detection and a good positive-negative coincidence rate of the detection results.

The present disclosure provides new anti-CD3 antibodies, including humanized ones, and their antigen-binding fragments. These antibodies can bind to both human and cynomolgus CD3 at high affinity, and their single chain fragments (scFv) can be readily incorporated into multispecific antibodies to effectively activate T cell in the presence of tumor cells. Further, even though a relatively small number, these antibodies have anti-CD3 activities of a broad range, which are accordingly categorized into nine different grades. As further demonstrated, these anti-CD3 antibodies and fragments can be suitably used in bi- or tri-specific antibodies to achieve optimized activities and safety margins.

The present invention provides recombinant bispecific antibodies designed to bind to a surface antigen on target cells and to an activating component on immune cells such as T cells. The bispecific antibodies comprise two polypeptide chains that contain Fv and Fab as antigen¬binding fragments and a modified Fc region to facilitate heterodimer formation. In one embodiment, the bispecific antibodies further comprise protease cleavage sites and / or motifs that would cause steric occlusion of the antigen binding sites so that the antibodies would be activated only in a specific environment, e.g. in the vicinity of a tumor. In another embodiment, the bispecific antibodies comprise modified sequences that confer reduced binding affinity to CDS and / or cross-reactive binding to CDS on cells from different species.

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.