120 results about "Complementarity determining region" patented technology

This invention relates to monoclonal antibodies for detecting A35R protein and their applications. This invention screened six antibodies, including antibody 4E7, antibody 11G12, antibody 6F10, antibody 6C11, antibody 18C3, and antibody 23A7. Specifically, this invention discloses the amino acid sequences of the heavy chain variable region and the light chain variable region of the above antibodies, as well as the amino acid sequences of their complementarity-determining regions and framework regions. Antibodies 4E7 and 11G12 can bind not only to the A35R-MPXV protein but also to its homologs A35R-CPXV, A35R-VTT8, and A35R-Variola. Antibodies 6F10, 6C11, 23A7, and 18C3 can specifically recognize the A35R-MPXV protein. The monoclonal antibodies described above all exhibit high binding capacity to the A35R protein, making them suitable for the sensitive and specific detection and prevention of monkeypox virus A35R protein. They can also be used clinically for the diagnosis and treatment of monkeypox virus infection-related diseases.

The application discloses a kind of nanobody specifically targeting human and murine NKG2D protein and its preparation method and application.The nanobody or antigen-binding fragment thereof of the application has three complementarity determining regions CDR1, CDR2 and CDR3;Wherein the amino acid sequences of CDR1, CDR2, CDR3 are as shown in SEQ ID NO.2, SEQ ID NO.3, SEQ ID NO.4 respectively.The nanobody can simultaneously bind hNKG2D and mNKG2D with high affinity, and the bispecific nanobody E5 / 2-B12 based on the nanobody can specifically bind CEACAM5 positive tumor cells and NKG2D overexpression cells, and effectively activate NK cells, which can significantly inhibit tumor growth and prolong survival in various tumor models, and has good application prospect in tumor immunotherapy.

The application discloses a shark-derived nanobody targeting FPV-VP2 protein and application thereof. The amino acid sequence of the complementarity determining region 3 of the shark-derived nanobody is selected from the sequence shown in any one of SEQ ID NO. 16 to SEQ ID NO. 30, or a sequence homologous to the sequence shown in any one of SEQ ID NO. 16 to SEQ ID NO. 30; or the amino acid sequence of the shark-derived nanobody is selected from the sequence shown in any one of SEQ ID NO. 1 to SEQ ID NO. 15, or a sequence homologous to the sequence shown in any one of SEQ ID NO. 1 to SEQ ID NO. 15. The shark-derived VNAR nanobody has the advantages of small molecular weight, high affinity, high stability, easy genetic engineering, low production cost and the like.

This invention discloses an anti-HIV antibody or a functional fragment thereof and its applications. The anti-HIV antibody or functional fragment disclosed in this invention includes a heavy chain complementarity-determining region and a light chain complementarity-determining region. This antibody or functional fragment has good specificity and sensitivity for HIV and can be used to detect human immunodeficiency virus (HIV) and for the diagnosis or auxiliary diagnosis of related diseases using HIV as a biomarker.

The application discloses a NbP2 single-domain antibody, a TAT-NbP2 fusion single-domain antibody and application thereof, and belongs to the technical field of biological medicines. The NbP2 single-domain antibody is composed of a framework region FR and three complementarity determining regions CDR1, CDR2 and CDR3, the amino acid sequence of the CDR1 is shown as SEQ ID NO. 1, the amino acid sequence of the CDR2 is shown as SEQ ID NO. 2, and the amino acid sequence of the CDR3 is shown as SEQ ID NO. 3. The TAT-NbP2 fusion single-domain antibody is a fusion protein of the NbP2 single-domain antibody and a TAT peptide segment of HIV-1 virus. The NbP2 single-domain antibody and the TAT-NbP2 fusion single-domain antibody provided by the application have dual activities of anti-virus and anti-inflammation, are safe, and provide a new idea for treating SARS-CoV-2 infection and developing anti-SARS-CoV-2 drugs.

The invention discloses an RTN4RL2 monoclonal antibody and an application of the RTN4RL2 monoclonal antibody. The monoclonal antibody provided by the invention can specifically target human RTN4RL2, and amino acid sequences of complementary determining regions CDR1, CDR2 and CDR3 of a heavy chain variable region of the monoclonal antibody are respectively shown as SEQ ID NO: 1, SEQ ID NO: 2 and SEQ ID NO: 3; amino acid sequences of complementary determining regions CDR1 and CDR3 of a light chain variable region are respectively shown as SEQ ID NO: 4 and SEQ ID NO: 5, and an amino acid sequence of a complementary determining region CDR2 is GAT. The monoclonal antibody can specifically bind to RTN4RL2 and has high affinity to RTN4RL2, in addition, T cell proliferation experiments show that the monoclonal antibody has a remarkable blocking effect on the T cell inhibition effect mediated by RTN4RL2, therefore, the monoclonal antibody can activate anti-tumor immune response by blocking the T cell inhibition effect of RTN4RL2, and a wide anti-tumor application prospect is shown.

This invention belongs to the field of biomedicine, and relates to single-domain antibodies, more specifically to a humanized single-domain antibody targeting VEGF and its applications. The amino acid sequence of the single-domain antibody includes three complementarity-determining regions (CDR1-CDR3) and four backbone regions (FR1-FR4). This invention also provides a recombinant protein containing the single-domain antibody, a nucleic acid molecule encoding the single-domain antibody or recombinant protein, a vector containing the nucleic acid molecule, a host cell containing the nucleic acid molecule or vector, and the application of the single-domain antibody or recombinant protein in the preparation of drugs targeting VEGF to treat diseases.

Provided herein are anti-Activin E antibodies having specific complementarity determining regions (CDRs) for the heavy and light chains, heavy and light chains, antigen binding fragments thereof, polynucleotides that encode the same, vectors, and host cells, and methods for treating a metabolic disorder, type 2 diabetes, obesity, an elevated triglyceride level, lipodystrophy, liver inflammation, fatty liver disease, hypercholesterolemia, an elevated liver enzyme, nonalcoholic steatohepatitis (NASH), a cardiovascular disease, cardiomyopathy, high blood pressure, and / or heart failure with the anti-Activin E antibodies disclosed herein.

The application discloses a nanobody 3A2 for human adenovirus and a preparation method and application thereof, and belongs to the technical field of biotechnology, and particularly relates to a nanobody 3A2 for human adenovirus and a preparation method and application thereof. The nanobody or antigen-binding fragment containing the nanobody for targeting human adenovirus has three complementarity determining regions CDR1, CDR2 and CDR3; the amino acid sequence of CDR1 is SEQ ID No. 1, the amino acid sequence of CDR2 is SEQ ID No. 2, and the amino acid sequence of CDR3 is SEQ ID No. 3. The nanobody 3A2 is fused with an Fc segment (hFc) of human immunoglobulin to obtain a fusion protein, and the obtained h3A2-hFc can effectively inhibit infection of human adenovirus type 55, and the IC 50 is 0.62 nM.

This invention relates to a human monoclonal neutralizing antibody targeting the metapneumovirus F protein and its applications. It comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region includes complementary determinant regions HCDR1, HCDR2, and HCDR3 as shown in SEQ ID NO:1, SEQ ID NO:2, and SEQ ID NO:3, respectively; and / or, the light chain variable region includes complementary determinant regions LCDR1, LCDR2, and LCDR3 as shown in SEQ ID NO:4, AAS, and SEQ ID NO:5, respectively. The metapneumovirus monoclonal neutralizing antibody MV32 of this invention can specifically bind to the metapneumovirus F antigen (approximately 0.6 nM) and exhibits good broad-spectrum neutralizing activity against representative strains such as hMPV A1, hMPV B1, and hMPV A2b. It also possesses certain in vivo protective and preventative effects and can be used for the prevention and treatment of human metapneumovirus infection, showing great application potential.

This application provides a monoclonal antibody combination against NFL protein and its uses. The monoclonal antibody combination includes a first antibody and a second antibody. The first antibody includes a first heavy chain variable region and a first light chain variable region, and the second antibody includes a second heavy chain variable region and a second light chain variable region. The first heavy chain variable region includes three complementarity-determining regions as shown in SEQ ID NO:3-5, the first light chain variable region includes three complementarity-determining regions as shown in SEQ ID NO:6-8, the second heavy chain variable region includes three complementarity-determining regions as shown in SEQ ID NO:11-13, and the second light chain variable region includes three complementarity-determining regions as shown in SEQ ID NO:14-16. The monoclonal antibody combination provided in this embodiment has excellent specificity and high affinity, and can be used for in vitro quantitative detection of serum NFL concentration, providing technical support for the auxiliary diagnosis of neurological diseases.

This invention provides an anti-BDCA-2 antibody, its applications, and products, belonging to the field of antibodies. The invention provides an anti-BDCA-2 antibody, whose light chain complementarity-determining region includes LCDR1, LCDR2, and LCDR3 as shown in SEQ ID NO: 25, WAS, and SEQ ID NO: 26; and its heavy chain complementarity-determining region includes HCDR1, HCDR2, and HCDR3 as shown in SEQ ID NO: 27, SEQ ID NO: 28, and SEQ ID NO: 29. The anti-BDCA-2 antibody and related drugs provided by this invention can be used to inhibit the production of IFN-α by pDCs, preventing excessive activation of pDCs. The anti-BDCA-2 antibody produced by this invention can effectively inhibit the activation of pDC cells and the production of IFN-α, showing great potential in resisting viral infections and preventing certain autoimmune diseases.

This invention relates to the field of biological detection, and more particularly to a monoclonal antibody combination for detecting human IL-8 protein and its application. The combination comprises monoclonal antibodies 2G3 and 3H8. The heavy and light chain variable regions of monoclonal antibody 2G3 include the complementarity-determining regions shown in SEQ ID NO. 1-6; the heavy and light chain variable regions of monoclonal antibody 3H8 include the CDRs shown in SEQ ID NO. 7-12. The antibody combination of this invention exhibits high specificity and effectively avoids cross-reactivity with other CXC chemokine family members, thereby significantly reducing non-specific background interference and the risk of false positives during detection. This invention provides a high-performance, quality-controllable key tool for biological detection for non-diagnostic purposes, research on inflammatory mechanisms, and the development of related scientific reagents.

A method for selecting camelid nanobodies from an array library collected from B cells of a camelid animal immunized with an antigen is provided. The method comprises (a) (i)phenylalanine (F) at position 42 (IMGT number), and (ii)a short hinge, and (iii)two or more cysteines in the nanobody sequence, and (iv)glutamine (Q) at position 123 (IMGT number), and (v)a low immunogenicity index, and (vi)a non-conventional VHH derived from germline IGHV3, or valine (V) included at position 42 (IMGT number), and (vii)a non-conventional VHH derived from germline IGHV4, or isoleucine (I) included at position 42 (IMGT number), and (viii)histidine (H), aspartic acid (D), or glutamic acid (E) in the CDR region, and (ix)histidine (H), aspartic acid (D), or glutamic acid (E) in the top 3 amino acid residues of the nanobody sequence, the FR2 region, or the top 16 amino acid residues of the FR3 region, and (x)tyrosine (Y) at position 42 (IMGT number), and a nanobody having a cyclic concave paratope structure arrangement, or (xi)phenylalanine (F) at position 42 (IMGT number), and a nanobody having a convex paratope structure arrangement, identifying a camelid nanobody having at least one of the features, and (b)measuring one or more biological activities of the nanobody identified in step (a).

The application belongs to the field of biological medicine, and relates to an anti-mouse integrin CD103 nanobody and application. The anti-mouse integrin CD103 nanobody comprises three complementarity determining regions CDR1, CDR2 and CDR3; wherein the amino acid sequence of CDR1 is a sequence or a high homology sequence shown in one of SEQ ID NO:1 to SEQ ID NO:4, the amino acid sequence of CDR2 is a sequence or a high homology sequence shown in one of SEQ ID NO:5 to SEQ ID NO:8, and the amino acid sequence of CDR3 is a sequence or a high homology sequence shown in one of SEQ ID NO:9 to SEQ ID NO:12. The application relates to the anti-mouse integrin CD103 nanobody and a preparation method thereof 18 The F-CYNB nanobody probe can realize targeted imaging of myocardial fibrosis, immune imaging of mouse tumors, and prediction of the effect of tumor immunotherapy.

This application belongs to the field of immunoassay technology, and discloses an aldosterone sandwich antibody mAb5 or its antigen-binding fragment, its preparation method, and its applications. The aldosterone sandwich antibody mAb5 or its antigen-binding fragment includes a light chain variable region (VL) and a heavy chain variable region (VH). The light chain variable region (VL) includes complementarity-determining regions (LCDR1, LCDR2, and LCDR3), whose amino acid sequences are shown in SEQ ID NO. 1-3, respectively. The heavy chain variable region (VH) includes complementarity-determining regions (HCDR1, HCDR2, and HCDR3), whose amino acid sequences are shown in SEQ ID NO. 4-6, respectively. Using the aldosterone sandwich antibody mAb5 of this application to detect aldosterone standard antigens, the detection sensitivity is less than 7 pg / mL. Magnetochemiluminescence immunoassay of clinical samples shows good correlation with clinical results within the sample range of 0-1000 pg / mL, which is of great significance in the diagnosis and treatment of essential hypertension and other aldosterone-related diseases.

The application belongs to the technical field of biological medicine, and particularly relates to an anti-FOLR1 nanobody and a preparation method and application thereof. The anti-FOLR1 nanobody comprises a framework region and a complementarity determining region, and the complementarity determining region amino acid comprises CDR1, CDR2 and CDR3. The application adopts automatic panning and a mammalian expression system, significantly improves the screening efficiency and antibody expression quality, greatly shortens the development cycle, and provides an efficient tool for FOLR1 targeted diagnosis and treatment. The obtained anti-FOLR1 nanobody exhibits excellent specific recognition and binding capacity.

The application provides an anti-CK8 nanobody, a polypeptide containing the nanobody and application thereof. A variable region in the amino acid sequence of the nanobody comprises three complementarity determining regions CDR and a framework region FR, the complementarity determining regions CDR comprising a complementarity determining region CDR1, a complementarity determining region CDR2 and a complementarity determining region CDR3, wherein the most important sites participating in antigen recognition and combination are RXXRXYX on the CDR1 and AASPAVSPPRDGRAFTY on the CDR3. The nanobody and the polypeptide thereof have high affinity and activity, can specifically recognize and combine CK8, and can be used for enrichment, removal and detection of CK8 and CK8 positive cells.

The application discloses a mechanism-driven nanobody-antigen binding prediction method and system, relates to the technical field of bio-information processing and artificial intelligence, and inputs amino acid sequences of nanobodies and antigens into a prediction system for processing, and a construction process of the prediction system comprises the following steps: after an encoder encodes the amino acid sequences of the nanobodies and the amino acid sequences of the antigens, global features and local features of respective complementarity determining regions are extracted and fused to obtain nanobody fusion features and antigen fusion features, and the nanobody fusion features and the antigen fusion features are subjected to global average pooling to obtain an encoder feature of the nanobodies and an encoder feature of the antigens; a combination prediction model models the interaction between the encoder feature of the nanobodies and the encoder feature of the antigens through Hadamard product modeling, generates an interaction feature, and predicts a combination probability based on the interaction feature. Through the cooperative work of the mechanism-driven encoder and the prediction system, high-precision and high-efficiency nanobody-antigen binding prediction is realized.

The application discloses a nanobody 2C10 for human adenovirus and a preparation method and application thereof, and belongs to the technical field of biotechnology, and particularly relates to a nanobody 2C10 for human adenovirus and a preparation method and application thereof. The nanobody or antigen-binding fragment containing the nanobody for targeting human adenovirus has three complementarity determining regions CDR1, CDR2 and CDR3; the amino acid sequence of CDR1 is SEQ ID No. 1, the amino acid sequence of CDR2 is SEQ ID No. 2, and the amino acid sequence of CDR3 is SEQ ID No. 3. The nanobody 2C10 is fused with an Fc segment (hFc) of human immunoglobulin to obtain a fusion protein, and the obtained h2C10-hFc can effectively inhibit infection of human adenovirus type 55, and the IC 50 is 5.33 nM.

This invention broadly relates to the field of bioassay technology, and more specifically, to a method for enriching exosomes and the conjugates used in this method. The conjugates are formed by conjugating a CD63 antibody or its antigen-binding fragment with a matrix support; wherein the heavy chain complementarity-determining regions HCDR1, HCDR2, and HCDR3 of the CD63 antibody or its antigen-binding fragment are shown in SEQ ID NO: 1-3, and the light chain complementarity-determining regions LCDR1, LCDR2, and LCDR3 of the antibody or its antigen-binding fragment are shown in SEQ ID NO: 4-6. The conjugates provided by this invention have high affinity and high purification efficiency, and show great promise for application in exosome purification.

The present disclosure relates generally to antibodies and functional binding fragments thereof that bind to programmed death-ligand 1 (PD-L1). In particular, the disclosed antibodies and fragments bind to human PD-L1 and comprise novel complementary determining regions (CDRs) also disclosed herein. Finally, the present disclosure relates to administering the disclosed antibodies and fragments to subjects with cancer, thereby treating or slowing the progression or proliferation of the cancer.

The present application relates to a kind of anti-procambarus clarkii white spot syndrome virus monoclonal antibody and its application, the complementary determining region CDR1-3 sequence of the heavy chain variable region of the anti-procambarus clarkii white spot syndrome virus monoclonal antibody is sequentially shown as SEQ ID NO:3-5, the complementary determining region CDR1-3 sequence of the light chain variable region is sequentially shown as SEQ ID NO:6-8.The present application successfully obtains the high affinity of anti-VP28 monoclonal antibody, and it has excellent affinity to procambarus clarkii white spot syndrome virus.The monoclonal antibody can be used for specific detection to procambarus clarkii white spot syndrome virus, and has good virus neutralization activity.By adding the monoclonal antibody in water body, the resistance of procambarus clarkii to white spot syndrome virus can be greatly improved, easy to operate, without injection, suitable for large-scale breeding scene, provide a new technical means for the prevention and control of white spot syndrome virus disease in aquaculture.

The application belongs to the technical field of biotechnology, and particularly relates to an anti-TL1A nanobody and application thereof. The amino acid sequences of the complementarity determining regions CDR1, CDR2 and CDR3 of the nanobody are respectively shown as SEQ ID NO:3, SEQ ID NO:4 and SEQ ID NO:5, and the amino acid sequence of the heavy chain variable region is shown as SEQ ID NO:1. The application uses a llama natural nanobody library and combines phage display technology to successfully screen a high-affinity nanobody targeting TL1A. The antibody can specifically recognize human TL1A protein and a TL1A overexpression cell line, and has high affinity, high specificity and good physicochemical stability. Based on the characteristic of targeting TL1A, the nanobody has important application value in the precise diagnosis and targeted treatment of TL1A high-expression related diseases such as inflammatory bowel disease, rheumatoid arthritis, asthma and fibrosis, and is particularly suitable for developing a high-sensitivity in-vitro diagnostic kit and a novel biological therapeutic drug.

The application belongs to the technical field of biological medicine, and particularly relates to an anti-CD22 nanobody and a preparation method and application thereof. The anti-CD22 nanobody comprises a framework region and a complementarity determining region, wherein the complementarity determining region comprises CDR1 (SEQ ID NO: 1), CDR2 (SEQ ID NO: 2) and CDR3 (SEQ ID NO: 3). The preparation method comprises the following steps: immunizing a llama with a Human CD22 / His protein, extracting RNA from PBMC cells and reverse transcribing the RNA into cDNA, constructing a phage display library, obtaining a positive clone through CD22 antigen protein panning after sequencing analysis, and expressing the antibody through a mammalian cell expression system. The application adopts an optimized phage display technology, has a short screening cycle, and the obtained nanobody has a small molecular weight, a stable structure and high affinity to CD22. The antibody can be efficiently expressed through a mammalian cell, and retains natural modification activity.

This application discloses an anti-human IL-17A protein monoclonal antibody, its preparation method, and its application. The anti-human IL-17A protein monoclonal antibody is mouse-derived and has a heavy chain complementarity-determining region as shown in SEQ ID NO. 1-3 and a light chain complementarity-determining region as shown in SEQ ID NO. 4-6. As a labeling antibody, this anti-human IL-17A protein monoclonal antibody can pair with monoclonal antibody 1E9 as a coating antibody to detect human IL-17A. It has high detection sensitivity and specificity and does not cross-react with other cytokine antigens, providing a raw material guarantee for the downstream development of high-quality diagnostic reagents.

The present disclosure provides scaffold proteins that serve as framework regions for different sets of complementarity determining regions (CDRs) from source antibodies, where the source antibodies bind to different epitopes. The scaffold proteins find use in generating antigen binding polypeptides in single chain fragment variable (scFv) antibody format from a variety of antibodies of interest. These antigen binding polypeptides can have one or more advantageous properties as compared to a source antibody, such as, increased affinity, increased stability, increased expression in a cell, increased yield, etc. The sequence of a scaffold protein has a sequence identity of less than 68% to the sequence of the framework regions of the source antibody.