27 results about "Cdr3 region" patented technology

The present disclosure provides a nanobody platform having a high affinity purification on protein A, wherein the nanobodies may incorporate diverse bioactive peptides, lipid or glycoside in its CDR1 and / or CDR3 regions. The present disclosure also provides a peptide-modified nanobody comprising non-toxic bioactive peptides and that exhibit potent anti-tumor activity. Moreover, the peptide-modified nanobody is able to be combined with other technologies, such as but not limited to bispecific antibodies and antibody-drug conjugates. Further, the present disclosure also provides production processes of the nanobodies and their use as a treatment and diagnostic agents.

The invention discloses a nano antibody specifically combined with CD176 protein and application thereof, the nano antibody sequentially comprises a CDR1 region, a CDR2 region and a CDR3 region, the amino acid sequence of the CDR1 region is shown as SEQ ID No.6, the amino acid sequence of the CDR2 region is shown as SEQ ID No.7, and the amino acid sequence of the CDR3 region is shown as SEQ ID No.8. The invention further discloses a preparation method of the nano antibody specifically combined with the CD176 protein and application of the nano antibody specifically combined with the CD176 protein. The invention discovers that the nano antibody with the three complementary determining regions can be combined with CD176 protein (EC50 is 8.617 nM) with high affinity, has the characteristics of small molecular weight, small immunogenicity, better solubility and stability and the like, can effectively detect the expression of CD176 or inhibit the activity of CD176, and has potential value in the aspects of tumor detection and treatment.

This invention relates to the field of antibodies, and more particularly to TAT antibodies and their applications. The invention provides coated antibodies comprising a heavy chain variable region and a light chain variable region, wherein: the CDR1, CDR2, and CDR3 regions of the heavy chain variable region have amino acid sequences as shown in SEQ ID No:1 to SEQ ID No:3; and the CDR1, CDR2, and CDR3 regions of the light chain variable region have amino acid sequences as shown in SEQ ID No:4 to SEQ ID No:6. This invention successfully prepared highly specific monoclonal antibodies 7E10 and 2B4 against the thrombin-antithrombin III complex (TAT), wherein 7E10 specifically binds to thrombin (THR), and 2B4 specifically binds to antithrombin III (AT-III). Using these two antibodies in combination enables highly sensitive and specific detection of the TAT complex.

The present application relates to a kind of artificially synthesized recombinant monoclonal antibody with human antibody amino acid sequence as framework.The present application uses phage display technology, and obtains one monoclonal antibody H11 from Tomlinson I+J phage library, and these new amino acid sequences constitute CDR1, CDR2 and CDR3 region, can be combined with A29L protein specific binding.It shows good stability, high specificity and high affinity and other characteristics, provide tool support for subsequent monkeypox virus diagnosis and detection with A29L protein as target.

A human immunoglobulin heavy chain transgene construct is provided that encodes a long CDR3 region. The heavy chain transgene comprises multiple VH regions that are longer than average and operably linked to multiple DD fusion segments. Transgenic animals containing the transgene are also provided. Methods for using the transgenic animals are also provided.

The application belongs to the technical field of biological medicine, and particularly relates to a TCR sequence targeting KRAS G12D antigen and application thereof. The CDR3 region of a wild type TCR is rationally designed and optimized through a simulation docking technology, and an optimized TCR with significantly improved affinity is obtained. Experimental results show that the TCR-T cell (human peripheral blood T cell TCR Homo sapiens) can effectively kill solid tumor cells, inhibit tumor growth in vivo and in vitro, improve the T cell immunotherapy effect, and can be used for preparing a cell drug for solid tumors, and has the advantages of high safety, strong targeting, significant effect and the like. The application provides a new drug selection and treatment scheme for the treatment of solid tumors.

The application discloses a kind of anti-SARS-CoV-2 virus monoclonal antibody 6G21H and its preparation method and application, the monoclonal antibody has the following shown heavy light chain CDR1, CDR2 and CDR3 region: heavy chain CDR1 region: DSPSDDYG;Heavy chain CDR2 region: ISYNGINK;Heavy chain CDR3 region: AKDSGPYYDIMIGYYDLNY;Light chain CDR1 region: QGISNY;Light chain CDR2 region: AAS;Light chain CDR3 region: QQYNSYPFT.The application belongs to the field of biotechnology, the monoclonal antibody provided by the application is designed to SAR-CoV-2 virus S protein, and rapid, specific detection of SAR-CoV-2 virus can be realized, easy to operate, and the stability and accuracy of detection result are good.

The invention relates to antigen-binding polypeptides comprising the CDR1, CDR2 and CDR3 region of a VHH domain of a camelid heavy chain antibody. The polypeptides bind specifically to CD229 and are therefore suitable for the diagnosis as well as for the therapeutic and prophylactic treatment of diseases characterised by increased CD229 expression. Fusion proteins, conjugates and pharmaceutical compositions comprising the antigen-binding polypeptides are also disclosed. In addition, the invention relates to the use of such antigenbinding polypeptides in methods for detecting CD229 or CD229-expressing cells in a biological sample. Methods for purifying and concentrating CD229 or CD229-expressing cells using the antigen-binding polypeptides are also described.

The present disclosure provides a nanobody platform having a high affinity purification on protein A, wherein the nanobodies may incorporate diverse bioactive peptides, lipid or glycoside in its CDR1 and / or CDR3 regions. The present disclosure also provides a peptide-modified nanobody comprising non-toxic bioactive peptides and that exhibit potent anti-tumor activity. Moreover, the peptide-modified nanobody is able to be combined with other technologies, such as but not limited to bispecific antibodies and antibody-drug conjugates. Further, the present disclosure also provides production processes of the nanobodies and their use as a treatment and diagnostic agents.

This invention discloses a nanobody and its application in the preparation of drugs for the treatment or diagnosis of CD176-positive tumor cancer. The nanobody sequentially comprises a CDR1 region, a CDR2 region, and a CDR3 region. The amino acid sequence of the CDR1 region is shown in SEQ ID No. 6, the amino acid sequence of the CDR2 region is shown in SEQ ID No. 7, and the amino acid sequence of the CDR3 region is shown in SEQ ID No. 8. This invention reveals that the nanobody possessing the above three complementarity-determining regions can bind to the CD176 protein (EC176) with high affinity. 50 With a molecular weight of 18.65 nM, it has the characteristics of small molecular weight, low immunogenicity, better solubility and stability, and can effectively detect the expression of CD176 or inhibit the activity of CD176, which has potential value in the detection and treatment of tumors.

This invention discloses a specific antibody for identifying K27 ubiquitin chains, belonging to the field of biomedical technology. The antibody is obtained through structural simulation, molecular docking, and site-directed mutagenesis, using the initial screening antibody zl1901 as a parent material. The optimal core strain is zl1901-R3-S8, whose light chain CDR1 and CDR2 regions can bind tightly to the receptor and donor ubiquitin of K27-diUb, while the heavy chain CDR3 region forms a specific hydrogen bond with the P19 residue of the K27-diUb donor ubiquitin. The antibody of this invention exhibits an affinity (KD) of 16.5 nM for K27-linked ubiquitin chains, shows no cross-binding with M1, K6, K11, K48, and K63-linked ubiquitin chains, and only exhibits a very weak binding with K29-diUb. This allows for precise identification of endogenous and exogenous K27-linked ubiquitination modifications, providing a core tool for studying the regulatory mechanism of K27 ubiquitination.

This invention discloses a nanobody that specifically binds to the CD176 protein and its applications. The nanobody sequentially comprises a CDR1 region, a CDR2 region, and a CDR3 region. The amino acid sequence of the CDR1 region is shown in SEQ ID No. 6, the amino acid sequence of the CDR2 region is shown in SEQ ID No. 7, and the amino acid sequence of the CDR3 region is shown in SEQ ID No. 8. This invention reveals that the nanobody possessing the above three complementarity-determining regions can bind to the CD176 protein (EC176) with high affinity. 50 With a molecular weight of 8.617 nM, it has the characteristics of small molecular weight, low immunogenicity, better solubility and stability, and can effectively detect the expression of CD176 or inhibit the activity of CD176, which has potential value in the detection and treatment of tumors.

The application belongs to the technical field of biological medicine, and particularly relates to a nano antibody against beta-catenin and a preparation method and application thereof. Specifically, the nano antibody with excellent affinity to beta-catenin is obtained through sample screening, has the advantages of small molecular weight (about 15 kilodaltons), small immunogenicity, better solubility and stability, and a long CDR3 region, thereby being beneficial to basic research and clinical experiments, having potential tumor diagnosis and treatment prospects, and thus having good practical application value.

The invention discloses a nano antibody and application thereof in preparation of a medicine for treating or diagnosing CD176 positive tumor cancers, the nano antibody sequentially comprises a CDR1 region, a CDR2 region and a CDR3 region, the amino acid sequence of the CDR1 region is shown as SEQ ID No.6, the amino acid sequence of the CDR2 region is shown as SEQ ID No.7, and the amino acid sequence of the CDR3 region is shown as SEQ ID No.8. The invention further discloses a preparation method of the nano antibody. The invention discovers that the nano antibody with the three complementary determining regions can be combined with CD176 protein (EC50 is 18.65 nM) with high affinity, has the characteristics of small molecular weight, small immunogenicity, better solubility and stability and the like, can effectively detect the expression of CD176 or inhibit the activity of CD176, and has potential value in the aspects of tumor detection and treatment.

The invention provides an anti-MERS nano antibody, a nano antibody fusion protein and application thereof, and belongs to the technical field of antibody drugs, the anti-MERS nano antibody comprises amino acid sequences of CDR1, CDR2 and CDR3 regions: CDR1: GSIFSRYT, CDR2: GSIFSRYT, CDR3: GSIFSRYT, GSIFSRYT: GSIFSRYT: GSIFSRYT: GSIFSRYT: CDR2 is an ITSEGNT (Intermediate Transcription Enhanced And CDR3 is NAGGGGAYFYHGAS. The nano antibody is obtained by screening through a phage display technology and has a unique CDR partition, and an antigen recognition epitope of the nano antibody is located in an RBD region of S1 protein. The anti-MERS nano antibody fusion protein provided by the invention has the characteristics of high expression, high stability, high specificity, high affinity, low immunogenicity and low-cost large-scale production, is suitable for industrial production, is expected to be used for coping with MERS pandemic potential crisis, and has great application value.

The invention belongs to the technical field of nano antibody libraries, and particularly relates to a random combinatorial library, an establishment method thereof and application of the random combinatorial library in screening of H9 subtype avian influenza virus nano antibodies. The library is obtained by connecting a fragment containing a CDR1 region, a fragment containing a CDR2 region and a fragment containing a CDR3 region which are respectively amplified by three pairs of PCR amplification primers, and the sequences of the three pairs of PCR amplification primers are respectively SEQ ID NO: 1-SEQ ID NO: 6. The positive rate of the library is 95.8%, and the capacity of the library is 2.7 * 10 < 9 >. In the library, the positive rate of the nano antibody capable of being combined with the H9 subtype avian influenza virus is 60%. According to the invention, the blank of the random combinatorial library aiming at the H9 subtype avian influenza virus nano antibody is filled, and a new way and strategy are provided for the establishment of the random combinatorial library aiming at the H9 subtype avian influenza virus nano antibody.

To provide antibodies that specifically bind to plasminogen activator inhibitor type 1 (PAI-1).SOLUTION: Provided are isolated monoclonal antibodies that specifically bind to PAI-1, comprising a heavy chain framework region and a heavy chain variable region, wherein the heavy chain variable region comprises a heavy chain CDR1 region comprising a specific sequence, a heavy chain CDR2 region comprising a specific sequence, and a heavy chain CDR3 region comprising a specific sequence, and a light chain framework region and a light chain variable region, wherein the light chain variable region comprises a light chain CDR1 region comprising a specific sequence, a light chain CDR2 region comprising a specific sequence, and a light chain CDR3 region comprising a specific sequence.SELECTED DRAWING: None

The invention relates to the technical field of biology, in particular to a nano antibody capable of being used for resisting porcine epidemic diarrhea virus S protein, fusion protein and application of the nano antibody and the fusion protein. The heavy chain variable region comprises three complementary determining regions CDR1, CDR2 and CDR3; the amino acid sequence of the CDR1, CDR2 and CDR3 of the nano antibody is selected from any one of the following items: (a) the amino acid sequence of the CDR1 is a sequence as shown in SEQ ID NO: 2, the amino acid sequence of the CDR2 is a sequence as shown in SEQ ID NO: 3, and the amino acid sequence of the CDR3 is a sequence as shown in SEQ ID NO: 4; (b) a variant comprising at most 5 amino acid substitutions in any one or more of the CDR1 region, CDR2 region and CDR3 region as compared to the amino acid sequence in (a). The nano antibody provided by the invention can be combined with the porcine epidemic diarrhea virus S protein with high affinity, and can be used for preparing medicines for preventing or treating porcine epidemic diarrhea virus infectious diseases.

The invention relates to the field of biotechnology and in vitro diagnosis, in particular to a recombinant monoclonal antibody of eosinophilic granulocyte peroxidase as well as preparation and application of the recombinant monoclonal antibody. The present invention provides an antibody that specifically binds to eosinophilic granulocyte peroxidase, which has a CDR1 region, a CDR2 region, and a CDR3 region. A pair of antibody pairs for specifically recognizing the eosinophilic granulocyte peroxidase is obtained through phage library screening, and the sensitivity of the pairs is higher, so that the eosinophilic granulocyte peroxidase is rapidly and accurately detected.

This invention discloses an alpaca-derived nanobody that binds to CD176 protein and its applications. The nanobody sequentially comprises CDR1, CDR2, and CDR3 regions, wherein the amino acid sequence of the CDR1 region is shown in SEQ ID No. 6, the amino acid sequence of the CDR2 region is shown in SEQ ID No. 7, and the amino acid sequence of the CDR3 region is shown in SEQ ID No. 8. This invention reveals that the nanobody possessing the above three complementarity-determining regions can bind to CD176 protein (EC176) with high affinity. 50 With a molecular weight of 62.07 nM, it has the characteristics of small molecular weight, low immunogenicity, better solubility and stability, and can effectively detect the expression of CD176 or inhibit the activity of CD176, which has potential value in the detection and treatment of tumors.

An antibody specifically binding to BCMA (B-cell maturation antigen) or fragment thereof, including: a heavy chain variable region including a CDR1 region represented by the amino acid sequence of SEQ ID NO: 1, a CDR2 region represented by the amino acid sequence of SEQ ID NO: 2, and a CDR3 region represented by the amino acid sequence of SEQ ID NO: 3; and a light chain variable region including a CDR1 region represented by the amino acid sequence of SEQ ID NO: 4, a CDR2 region represented by the amino acid sequence of SEQ ID NO: 5, and a CDR3 region represented by the amino acid sequence of SEQ ID NO: 6.

The invention discloses an alpaca-derived nano antibody combined with CD176 protein and application thereof, the nano antibody sequentially comprises a CDR1 region, a CDR2 region and a CDR3 region, the amino acid sequence of the CDR1 region is shown as SEQ ID No.6, the amino acid sequence of the CDR2 region is shown as SEQ ID No.7, and the amino acid sequence of the CDR3 region is shown as SEQ ID No.8. The invention further discloses a preparation method of the alpaca-derived nano antibody combined with the CD176 protein and application of the alpaca-derived nano antibody combined with the CD176 protein. The invention discovers that the nano antibody with the three complementary determining regions can be combined with CD176 protein (EC50 is 62.07 nM) with high affinity, has the characteristics of small molecular weight, small immunogenicity, better solubility and stability and the like, can effectively detect the expression of CD176 or inhibit the activity of CD176, and has potential value in the aspects of tumor detection and treatment.

The present disclosure provides T cell receptors comprising an antigen binding variable region that specifically binds an antigenic peptide derived from SF3B1 K700E. The present disclosure further provides activated or engineered T cells comprising the T cell receptors of the disclosure, and methods of making and using these T cell receptors. Aspects of the disclosure further relate to a polypeptide comprising an antigen binding variable region comprising a CDR3 region of the disclosure.

Provided is a set of shark nanobodies targeting an infectious hypodermal and haematopoietic necrosis virus of shrimp. The amino acid sequence of each nanobody in the set is selected from any one of SEQ ID NOs. 8-14. The nanobodies are useful for detecting cp, nsp1, and nsp2 antigens of the infectious hypodermal and haematopoietic necrosis virus. A preparation or screening method for the nanobodies comprises the following steps: step A: expression and purification of cp, nsp1, and nsp2 antigens; step B: construction of a shark naive library and / or a shark immune library; step C: helper phage rescue and purification to obtain a phage library; step D: panning of anti-cp, anti-nsp1, and anti-nsp2 antigen phage libraries; and step E: identification by phage-ELISA and sequencing, and sequence alignment to obtain cp, nsp1, and nsp2 nanobodies having different CDR3 region sequences.

The invention provides an immune disease risk assessment method. The method comprises the following steps: acquiring TCR sequence data of each sample in a training set and a test set; the TCR sequence data comprises data obtained by embedding an amino acid sequence of each high-expression TCR [beta] CDR3 after quality control into a high-dimensional vector through a pre-trained protein language model; obtaining the risk score of the immune disease of the corresponding object through a convolutional neural network by using the TCR sequence data of the training set and the test set; through a multi-fold cross validation training model, calculating indexes of the trained model of each fold, and selecting an optimal model as a risk prediction model of the immune disease based on the F1 value; and obtaining TCR sequence data of the detected object, and inputting the TCR sequence data into the risk prediction model for risk assessment to obtain the risk score of the immune disease of the detected object. The method focuses on a CDR3 region of a TCR beta chain, and comprehensively reflects the core effect of T cells in immune response and close association of the T cells with immune diseases.

The present disclosure provides a nanobody platform having a high affinity purification on protein A, wherein the nanobodies may incorporate diverse bioactive peptides, lipid or glycoside in its CDR1 and / or CDR3 regions. The present disclosure also provides a peptide-modified nanobody comprising non-toxic bioactive peptides and that exhibit potent anti-tumor activity. Moreover, the peptide-modified nanobody is able to be combined with other technologies, such as but not limited to bispecific antibodies and antibody-drug conjugates. Further, the present disclosure also provides production processes of the nanobodies and their use as a treatment and diagnostic agents.