30 results about "Antibody screens" patented technology

The invention discloses an anti-B7-H3 antibody as well as a preparation method, conjugate and application thereof. The anti-B7-H3 antibody comprises a complementary determining region which is one ormore of a heavy chain CDR1, a heavy chain CDR2 and a heavy chain CDR3, and / or, one or more of a light chain CDR1, a light chain CDR2 and a light chain CDR3, and a sequence is as described in the invention. The anti-B7-H3 antibody disclosed by the invention is a fully humanized antibody screened from a phage library, and has a unique antigen binding epitope; and the antibody can specifically bind to a B7-H3 antigen on a tumor cell, can be quickly internalized into the cell after binding to the tumor cell, can be used for ADC drug development, and is expected to obtain the better antitumor activity and efficacy so as to achieve the purpose of treating cancers.

The invention relates to a cell strain for screening affinity maturation of an antibody and a use method thereof. The cell strain is stable in expression of a target antibody by virtue of a RMCE technology. Combined with a somatic hypermutation technology of activation-induced cytidine deaminase, the cell strain for screening affinity maturation of the antibody is relatively high in efficiency and the affinity of the antibody can be improved to a great extent within a relatively short time and screening turns.

The invention provides an anti-PD-L1 nano antibody and application thereof. The sequence of the antibody comprises an FR region, a CDR region and an HV region, wherein the FR region comprises an FR1 region with an amino acid sequence as shown in SEQ ID NO.1, an FR2 region with an amino acid sequence as shown in SEQ ID NO.2, an FR3 region with an amino acid sequence as shown in SEQ ID NO.3 and an FR4 region with an amino acid sequence as shown in SEQ ID NO.4; the CDR region comprises a CDR1 region with an amino acid sequence shown as SEQ ID NO.5 and a CDR3 region with an amino acid sequence shown as any one of SEQ ID NO.8 to SEQ ID NO.12; and the HV region comprises an HV2 region with an amino acid sequence as shown in SEQ ID NO.6 and an HV4 region with an amino acid sequence as shown in SEQ ID NO.7. The anti-PD-L1 nano antibody screened on the basis of the novel shark V-NAR framework sequence has excellent stability and can provide a new variety for research, development and acquisition of novel antitumor drugs.

Belonging to the field of biotechnologies, the invention relates to a screening method for a paraquat simulation antibody and application thereof. The simulation antibody is screened out from a ribosome display Lipocalin simulation antibody library and is subjected to soluble functional expression. The invention also relates to a method of screening the paraquat simulation antibody by a ribosome display technology. The paraquat simulation antibody screened out in the invention can be used for paraquat residual monitoring and development of a kit for rapid detection of pesticide paraquat residual.

The present invention relates to a method for constructing an Fv library based on a combination of proteins, a method of screening a desired antibody using the constructed Fv library, an Fv antibody screened by the screening method, and an Fv library constructed by the Fv library construction method. The Fv library of the present invention is based on a combination of proteins so that members thereof can be individually analyzed for their function. Moreover, the Fv library enables a desired Fv antibody to be screened without needing a target antigen preparation. In addition, the protein combination based Fv library makes it possible to significantly reduce the number of protein purification processes to thereby reduce costs and time, compared to conventional DNA-based libraries.

The invention relates to a diethylstilbestrol single-chain antibody screening method and a purpose of a diethylstilbestrol single-chain antibody, and belongs to the technical field of biology. The single-chain antibody is screened from a ribosome showing mouse source natural antibody base and is subjected to soluble expression. The invention further relates to a diethylstilbestrol antibody screening method with a ribosome showing technology. The diethylstilbestrol single-chain antibody screened through the method can be used for pollution detection, development of immune quick test kits used for quick test of diethylstilbestrol residual and treatment of relevant diseases, and a foundation is laid for future detection and research on the diethylstilbestrol single-chain antibody.

The invention provides an anti-CD123 nano antibody and application thereof. The nano antibody comprises a heavy chain variable region, wherein the heavy chain variable region comprises CDR1 as shown in SEQ ID NO: 1, CDR2 as shown in SEQ ID NO: 2 and CDR3 as shown in SEQ ID NO: 3. The antibody screened from the camel VHH immune library has CDR regions shown as SEQ ID NO: 1-3, the nano antibody formed by combining the antibody with different framework regions FR has strong affinity with CD123, so that the constructed chimeric antigen receptor and chimeric antigen receptor immune cells have remarkable cytotoxicity on CD123 positive cells, and have wide application prospects in the field of tumor treatment.

The present invention relates to a method known as Tat-related protein transformation engineering (TAPE), wherein a target protein and an antibiotic resistance protein are linked to a Tat signal sequence, the obtained substance is expressed in Escherichia coli, the target protein with advantages of high solubility and excellent heat stability is screened, and particularly human or modified VH and VL domain antibody and a human or modified VH and VL domain antibody scaffold derived from the immunoglobulin variable domain (VH or VL) of human germ cells, screened by the TAPE method and having advantages of solubility and excellent thermal stability are screened. The invention further provides a library and a preparation method thereof, wherein the library has a human or modified VH and VL domain antibody or antibody scaffold screened by the TAPE method and containing a random CDR sequence. The invention further provides a VH or VL domain antibody screened by the library and having target protein binding ability, and a pharmaceutical composition containing the domain antibody.

The invention belongs to the field of biotechnology, and relates to an antibody and development and production of the antibody, in particular to a monoclonal ScFv antibody phage library for resisting mouse RCN3 protein as well as a selecting method of the monoclonal ScFv antibody. The base sequence of the monoclonal ScFv antibody is shown in SEQ ID NO: 10 and the amino acid sequence corresponding to the base sequence is shown in SEQ ID NO:9. The invention discloses construction and selecting methods of the antibody phage library which has high affinity to mouse RCN3 protein, is displayed on phage surfaces and can be used for efficient screening, sequences of the antibody and eukaryotic expression and antigen detection methods. The ScFv antibody which can realize specific recognition and combines the mouse RCN3 protein molecules can be selected with the selecting method, and the antibody screened by the construction and selecting methods has wide application prospect for detection and disease control related to RCN3 protein.

The invention provides a nano antibody for resisting a B cell maturation antigen and an application of the nano antibody. A heavy chain variable region of the nano antibody for resisting the B cell maturation antigen comprises a complementary determining region 1 as shown in SEQ ID NO. 1, a complementary determining region 2 as shown in SEQ ID NO. 2 and a complementary determining region 3 as shown in SEQ ID NO. 3. The antibody screened by using a phage display nano antibody library has a specific CDR region, and the obtained antibody can be specifically bound with a BCMA antigen and has good affinity; When being used as an antigen binding structural domain to construct a chimeric antigen receptor and a CAR-T cell, the antibody has obvious killing activity on BCMA positive tumor cells. Therefore, the nano antibody has a wide application prospect in the aspect of immunotherapy of multiple myeloma.

The invention provides a nano-antibody for resisting a B cell maturation antigen and application of the nano-antibody. The nano-antibody for resisting the B cell maturation antigen is BCMA-12, and a heavy chain variable region of the BCMA-12 comprises a complementary determining region 1 as shown in SEQ ID NO. 1, a complementary determining region 2 as shown in SEQ ID NO. 2 and a complementary determining region 3 as shown in SEQ ID NO. 3. The nano-antibody screened by using a phage display nano-antibody library has a specific CDR region, and the obtained nano-antibody can specifically bind to a BCMA antigen and has good affinity; when being used as an antigen binding structural domain to construct a chimeric antigen receptor and a CAR-T cell, the nano-antibody has obvious killing activity on BCMA-positive tumor cells; and therefore, the nano-antibody has wide application prospects in the aspect of immunotherapy of multiple myeloma.

The invention provides an antibody for resisting a B cell maturation antigen and application of the antibody. The antibody is BCMA-21, and a heavy chain variable region of the antibody comprises a complementary determining region 1 as shown in SEQ ID NO. 1, a complementary determining region 2 as shown in SEQ ID NO. 2 and a complementary determining region 3 as shown in SEQ ID NO. 3. The antibody screened by utilizing a phage display nano antibody library has a specific CDR region, can specifically bind to a BCMA antigen with good affinity, and has Ka (1 / Ms) of 7.48E+06, Kd (1 / s) of 8.50E-04, and KD (M) of 1.14E-10. A chimeric antigen receptor and CAR-T cell can be constructed by using the antibody as the antigen-binding domain, and have obvious killing activity on BCMA-positive tumor cells.

The invention discloses a preparation method for a recombinant rabbit monoclonal antibody. The method utilizes immune-raised rabbit B cells for isolation, phage display and other technologies, antibody gene fragments are amplified through specific primers, an antibody library is constructed, an antigen is used for panning to obtain positive clones, sequence identification is performed to obtain heavy and light chain sequences, in-vitro recombinant expression is performed, and the antibody is measured; compared with a traditional method for preparing a monoclonal antibody, the preparation method for the monoclonal antibody provided by the invention is higher in efficiency of preparing the monoclonal antibody and more convenient to operate; and compared with a mouse monoclonal antibody, themonoclonal antibody screened by using an immune system of an experimental rabbit and capable of recognizing a specific antigen has the prominent characteristics of high affinity and more abundant recognized epitopes, and can recognize antigens having no immunogenicity in mice.

The invention provides a hybridoma cell strain A4-1B1, a procalcitonin monoclonal antibody generated by the same, and an application of the procalcitonin monoclonal antibody. The hybridoma cell strainA4-1B1 is preserved in China Center for Type Culture Collection with the preservation number of CCTCC NO:C2017144. The procalcitonin monoclonal antibody can be applied to an immunoassay method. The present invention also provides a group of paired antibodies. The group of paired antibodies is composed of the antibody generated by the hybridoma cell strain A4-1B1 and an antibody generated by a hybridoma cell strain A4-6A2, and the hybridoma cell strain A4-6A2 is preserved in China Center for Type Culture Collection with the preservation number of CCTCC NO:C2017143. The antibodies provided by the invention have the advantages of high specificity, sensitiveness in reaction, and low cost, and can reflect the active state of infection. The anti-PCT monoclonal antibodies 1B1 and 6A2 are the optimal paired antibodies screened by a double-antibody sandwich method.

The invention provides a monoclonal antibody for resisting a B cell maturation antigen and an application of the monoclonal antibody. A heavy chain variable region of the monoclonal antibody for resisting the B cell maturation antigen comprises a complementary determining region 1 as shown in SEQ ID NO. 1, a complementary determining region 2 as shown in SEQ ID NO. 2 and a complementary determining region 3 as shown in SEQ ID NO. 3. The antibody screened by using a phage display nano-antibody library has a specific CDR region, the obtained antibody can be specifically bound with a BCMA antigen, the affinity is good, the Ka(1 / Ms) is 3.03E+06, the Kd(1 / s) is 2.14E-04, and the KD(M) is 7.09E-11. Therefore, the monoclonal antibody has a wide application prospect in the aspect of immunotherapy of multiple myeloma.

The present invention provides a nanobody against B cell maturation antigen and its application. The heavy chain variable region of the anti-B cell maturation antigen Nanobody includes: the complementarity determining region 1 shown in SEQ ID NO.1, the complementarity determining region 2 shown in SEQ ID NO.2 and the complementarity determining region shown in SEQ ID NO.3. Complementarity determining region 3 shown. In the present invention, the antibody screened by the phage display nanobody library has a specific CDR region, and the obtained antibody can specifically bind the BCMA antigen with good affinity; it is used as the antigen binding domain to construct a chimeric antigen receptor and CAR-T It has obvious killing activity to BCMA-positive tumor cells. Therefore, the nanobody has broad application prospects in the immunotherapy of multiple myeloma.

The invention discloses a human anti-Siglec-15 antibody and an application thereof. The human anti-Siglec-15 antibody screened through a phage antibody library technology can be combined with cells expressing human Siglec-15 antigens in a high-specificity mode, the preparation method of the targeted human Siglec-15 antibody is simple, the use of a hybridoma technology is avoided, and the obtained anti-human Siglec-15 antibody can well detect Siglec-15 protein expressed on tumor cells. The targeted human Siglec-15 antibody disclosed by the invention is high in specificity and has a very good prospect in application to treatment and / or prevention or diagnosis of Siglec-15 related diseases such as tumors.

The invention discloses a bovine viral diarrhea virus differential detection test strip and a preparation method thereof, which are used for rapid and sensitive detection of BVDV antibodies. The test strip is composed of a support base plate, a coated adsorption material layer, a protein marker bearing material layer, a sample buffer material layer, a liquid absorbent material layer, and an outer protective material; the coated absorbent material is provided with a test line and a quality control line The protein label of the test strip is labeled with colloidal gold; the protein used for the protein label is the phage monoclonal combined with the BVDV antibody obtained by screening from the phage polypeptide library; the polypeptide epitope expressed by the phage monoclonal is LTPHKHHKHLHA. The preparation method comprises the preparation of gold-labeled phage monoclonal, the preparation of gold-labeled pads, the preparation of nitrocellulose membrane, and the assembly of various parts to obtain the finished product. The invention can obtain detection results within ten minutes, is fast and sensitive, has low cost, is simple to operate, and is easy to be popularized and applied in production and scientific research at the grassroots level.

The present invention provides an anti-CD123 nanobody and application thereof, the nanobody comprises a heavy chain variable region; the heavy chain variable region comprises CDR1 shown in SEQ ID NO: 1 and CDR2 shown in SEQ ID NO: 2 , and CDR3 shown in SEQ ID NO:3. The antibodies screened from the camel VHH immune library of the present invention have the CDR regions shown in SEQ ID NOs: 1 to 3, and the nanobodies formed by combining with different framework regions FR have strong affinity with CD123, and the chimeric antigen receptor constructed by this , Chimeric antigen receptor immune cells have significant cytotoxicity to CD123 positive cells, and have broad application prospects in the field of tumor therapy.

The current disclosure provides compositions, systems, and methods for detection and / or identification of antibodies. Also provided are compositions, systems, and methods that expedite and simplify processes to identify blood units that are clinically appropriate for transfusion into a recipient, and more generally to identify the presence of antibody(s) in blood that are specific for selected antigen(s). The systems and methods utilize genetically-modified (transgenic) non-target-organism red blood cells that express at least one antigen of the target organism species. This enables screening and identifying blood units faster, more consistently, at large scale, and / or with less dependence on human involvement.

The present invention provides an antibody against B cell maturation antigen and its application. The antibody of described anti-B cell maturation antigen is BCMA-21, and its heavy chain variable region includes: complementarity determining region 1 shown in SEQ ID NO.1, complementarity determining region 2 shown in SEQ ID NO.2 and SEQ ID NO.2 Complementarity determining region 3 shown in NO.3. In the present invention, the antibody screened by the phage display nanobody library has a specific CDR region, and the obtained antibody can specifically bind to the BCMA antigen with good affinity, and its K a (1 / Ms) is 7.48E+06, K d (1 / s) for 8.50E‑04, K D (M) is 1.14E-10, which is used as an antigen-binding domain to construct chimeric antigen receptors and CAR-T cells, which have obvious killing activity to BCMA-positive tumor cells.

The present invention provides an anti-BCMA antigen-binding fragment and its application. The heavy chain variable region of the antigen-binding fragment of the anti-B cell mature antigen includes: the complementarity determining region 1 shown in SEQ ID NO.1, the complementarity determining region 2 shown in SEQ ID NO.2 and the complementarity determining region shown in SEQ ID NO.3. Complementarity determining region 3 shown. In the present invention, the antibody screened by the phage display antigen-binding fragment library has a specific CDR region, and the obtained antibody can specifically bind to the BCMA antigen, and has good affinity, and its K a (1 / Ms) is 2.81E+06, K d (1 / s) is 4.36E‑04, K D (M) is 1.55E-10; it is used as an antigen-binding domain to construct chimeric antigen receptors and CAR-T cells, which has broad application prospects in the immunotherapy of multiple myeloma.

The invention provides an anti-BCMA antigen binding fragment and application thereof. A heavy chain variable region of the antigen binding fragment of the anti-B cell maturation antigen comprises a complementary determining region 1 as shown in SEQ ID NO. 1, a complementary determining region 2 as shown in SEQ ID NO. 2 and a complementary determining region 3 as shown in SEQ ID NO. 3. The antibody screened by using a phage display antigen binding fragment library has a specific CDR region, the obtained antibody can be specifically bound with a BCMA antigen, the affinity is good, the Ka (1 / Ms) is 2.81 E + 06, the Kd (1 / s) is 4.36 E-04, and the KD (M) is 1.55 E-10; when being used as an antigen binding structural domain to construct a chimeric antigen receptor and a CAR-T cell, the anti-BCMA antigen binding fragment has a wide application prospect in the aspect of immunotherapy of multiple myeloma.

The invention discloses a fully human antagonistic antibody screened from a ScFv phage antibody library with THY-1 / CD90 as a target, the fully human antagonistic antibody is a single-chain antibody, and the heavy chain DNA sequence of the fully human antagonistic antibody As shown in SEQ ID NO:1, the light chain DNA sequence is shown in SEQ ID NO:2, the heavy chain amino acid sequence is shown in SEQ ID NO:3, and the light chain amino acid sequence is shown in SEQ ID NO:4. According to the above technical scheme, the fully human antagonistic antibody targeting THY-1 / CD90 is screened from the human ScFv phage antibody library, and its DNA sequence and amino acid sequence are respectively determined. The fully human antagonistic antibody obtained by this method has the target Specificity towards THY‑1 / CD90. The antibody produced in this way can overcome the shortcomings of hybridoma technology to produce antibodies, and can also achieve the purpose of high-throughput and rapid screening of antibodies, and the price is low.

The invention discloses an anti-drug antibody combined with a coronavirus bispecific antibody, a preparation method and application thereof. The anti-drug antibody comprises a heavy chain variable region and a light chain variable region, the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3, wherein each functional region See the present invention for details of the sequence. The anti-drug antibody screened by the invention has high binding affinity and specificity.

The present invention provides a nanobody against B cell maturation antigen and its application. The anti-B cell maturation antigen nanobody is BCMA-12, and the heavy chain variable region of the BCMA-12 includes: complementarity determining region 1 shown in SEQ ID NO.1, complementarity determining region 1 shown in SEQ ID NO.2 Determining region 2 and complementarity determining region 3 shown in SEQ ID NO.3. In the present invention, the antibody screened by the phage display nanobody library has a specific CDR region, and the obtained antibody can specifically bind to the BCMA antigen with good affinity; it is used as the antigen binding domain to construct a chimeric antigen receptor and CAR-T It has obvious killing activity to BCMA-positive tumor cells. Therefore, the nanobody has broad application prospects in the immunotherapy of multiple myeloma.

The present invention relates to a method for constructing an Fv library based on a combination of proteins, a method of screening a desired antibody using the constructed Fv library, an Fv antibody screened by the screening method, and an Fv library constructed by the Fv library construction method. The Fv library of the present invention is based on a combination of proteins so that members thereof can be individually analyzed for their function. Moreover, the Fv library enables a desired Fv antibody to be screened without needing a target antigen preparation. In addition, the protein combination based Fv library makes it possible to significantly reduce the number of protein purification processes to thereby reduce costs and time, compared to conventional DNA-based libraries.

The invention belongs to the field of biotechnology, and relates to an antibody and development and production of the antibody, in particular to a monoclonal ScFv antibody phage library for resisting mouse RCN3 protein as well as a selecting method of the monoclonal ScFv antibody. The base sequence of the monoclonal ScFv antibody is shown in SEQ ID NO: 10 and the amino acid sequence corresponding to the base sequence is shown in SEQ ID NO:9. The invention discloses construction and selecting methods of the antibody phage library which has high affinity to mouse RCN3 protein, is displayed on phage surfaces and can be used for efficient screening, sequences of the antibody and eukaryotic expression and antigen detection methods. The ScFv antibody which can realize specific recognition and combines the mouse RCN3 protein molecules can be selected with the selecting method, and the antibody screened by the construction and selecting methods has wide application prospect for detection and disease control related to RCN3 protein.

The present invention provides a chimeric antigen receptor against human CAIX antigen and its application; the chimeric antigen receptor consists of a scFv recognizing human CAIX antigen, a hinge region, a transmembrane region and an intracellular signal domain in sequence. A new anti-human CAIX scFv was screened by a hybridoma antibody screening system, and the scFv was concatenated with the Hinge and transmembrane region of human CD8, the intracellular signaling domain of 4‑1BB and CD3ζ to construct a new chimeric antigen receptor scFv‑CD8‑4‑1BB‑CD3ζ, with higher specificity and better tumor killing effect.

The present invention provides an anti-CD123 antibody and use thereof, the antibody includes a heavy chain variable region; the heavy chain variable region includes CDR1 shown in SEQ ID NO: 1, CDR2 shown in SEQ ID NO: 2, and CDR3 shown in SEQ ID NO:3. The antibodies screened from the camel VHH immune library of the present invention have the CDR regions shown in SEQ ID NOs: 1 to 3, and the antibodies formed by combining with the framework region FRs have strong affinity for CD123, and the chimeric antigen receptors, chimeric antigen receptors and chimeric antigen receptors constructed thereby Antigen receptor immune cells have significant cytotoxicity to CD123 positive cells and have broad application prospects in the field of tumor therapy.