70 results about "Framework region" patented technology

The invention discloses a T-2 toxin monoclonal antibody and application thereof, and belongs to the technical field of biology. The monoclonal antibody contains a heavy chain variable region and a light chain variable region, the heavy chain variable region and the light chain variable region are both composed of complementary determining regions and frame regions, and the complementary determining regions are both composed of CDR1, CDR2 and CDR3. The monoclonal antibody can be used for preparing a T-2 toxin detection product. The T-2 toxin colloidal gold test strip provided by the invention has the characteristics of high sensitivity, good specificity and strong stability.

The embodiment of the invention discloses an antibody generation method and device, computer equipment and a storage medium, and belongs to the technical field of computers. The method comprises the following steps: acquiring antigen information and frame region information, wherein the antigen information indicates amino acid in an antigen; performing feature extraction on the antigen information and the frame region information to obtain a first feature and a second feature; the first feature and the second feature are decoded, first antibody information is obtained, an antibody indicated by the first antibody information is used for being combined with the antigen, and the antibody comprises a frame area indicated by the frame area information. According to the invention, the stability and reliability of the antibody are ensured, the antibody information can be quickly generated aiming at the specific antigen information, the antibody generation efficiency is improved, the framework area can be specified for the antibody to be generated, the personalized configuration of the generated antibody is ensured, and the flexibility of antibody generation is ensured.

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 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.

This invention provides low-viscosity antigen-binding proteins and methods for producing them. [Solution] The present invention relates to a method for reducing the viscosity of an antigen-binding protein by modifying the sequence in the framework region and / or Fc domain, which has been shown to be associated with high viscosity. The present invention provides antigen-binding proteins, particularly antibodies, that have been mutated to reduce viscosity. Preferred antigen-binding proteins according to the present invention include antibodies, as shown in Figure 1B, having one or more, preferably all, of the following: VH1|1-18 germline subfamily substitution; VH3|3-33 germline subfamily substitution; VK3|L16 germline subfamily substitution; VK3|L6 germline subfamily substitution; or Fc substitution.

The application discloses a spiramycin monoclonal antibody and application thereof, and belongs to the technical field of biology. The monoclonal antibody contains a heavy chain variable region and a light chain variable region, the heavy chain variable region and the light chain variable region are both composed of a complementarity determining region and a framework region, and the complementarity determining region is composed of CDR1, CDR2 and CDR3. The monoclonal antibody can be used for preparing a spiramycin detection preparation. The spiramycin colloidal gold detection test strip provided by the application has the characteristics of high sensitivity, good specificity and strong stability.

Aspects of the disclosure relate to PD-1 binding proteins comprising immunoglobulin domains which bind specifically to PD-1 and comprise at least three or six specific complementarity determining regions (CDRs) and which comprise a specific feature in a variable domain framework region(s), e.g., heavy variable domain framework 1, heavy domain framework 4, and / or light chain variable domain framework 3 region(s). In some embodiments, the PD-1 protein comprises the substitution(s) L108G and / or T110R of the heavy chain reference sequence and / or I58R relative to the light chain reference sequence(s). The PD-1 binding proteins are useful, e.g., as immunologic adjuvants, for detecting and quantifying PD-1, monitoring patient responses to therapies, diagnosing PD-1 related conditions, and treating or preventing disorders involving PD-1 expressing cells, such as, e.g., cancers and autoimmune diseases. Also provided herein are antigen binding proteins comprising amino acid substitutions in the heavy chain framework 4 region for improved stability and solubility.

The invention belongs to the technical field of biological medicines, and particularly relates to an anti-CD22 nano antibody as well as a preparation method and application thereof. The anti-CD22 nano antibody 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 alpaca by using Human CD22 / His protein, extracting RNA (Ribonucleic Acid) from PBMC (Peripheral Blood Mononuclear Cell) and reversely transcribing into cDNA (Complementary Deoxyribose Nucleic Acid), constructing a phage display library, then performing CD22 antigen protein elutriation to obtain positive clone, and after sequencing analysis, expressing the antibody by using a mammalian cell expression system. The optimized phage display technology is adopted, the screening period is short, and the obtained nano antibody is small in molecular weight, stable in structure and high in affinity to CD22. The antibody can be efficiently expressed through mammalian cells, and natural modification activity is reserved.

Human or chimeric heavy chain-only antibodies are provided, in the native amino acid residue at the first position of the fourth framework region (FR4) of said HCAb is substituted by a different amino acid residue that is capable of disrupting a surface-exposed hydrophobic patch comprising or associated with the native amino acid residue at that position.

The application provides a non-pH-dependent long-acting anti-serum albumin nanobody and an application thereof. Specifically, the application provides amino acid sequences of VHH chain framework regions FR and complementarity determining regions CDR of the non-pH-dependent long-acting anti-serum albumin nanobody. The application also provides nucleotide sequences encoding the nanobody. The anti-serum albumin nanobody provided by the application can bind to human, mouse, rat and cynomolgus serum albumin under different pH conditions, and can significantly prolong the half-life of a protein drug, thereby providing a research basis for long-acting protein drug development.

The present invention belongs to the technical field of biomedicine. Provided are a nanobody targeting IL-23A and the use thereof. The nanobody comprises a framework region and a complementarity determining region, wherein the framework region comprises FR-H1, FR-H2, FR-H3 and FR-H4 having amino acid sequences as shown in SEQ ID NOs. 4-7, respectively; and the complementary determining region comprises CDR-H1, CDR-H2 and CDR-H3 having amino acid sequences as shown in SEQ ID NOs. 1-3, respectively. The nanobody can be used in the preparation of an antibody drug targeting IL-23A, which is capable of treating related diseases by means of binding to IL-23A.

The present invention discloses a nanobody targeting IL-23A and an application thereof, and relates to the technical field of biological medicine. The nanobody VVH1 includes framework regions and complementary determining regions; the framework regions include VVH1FR-H1, VVH1FR-H2, VVH1FR-H3 and VVH1FR-H4, and the amino acid sequences of VVH1FR-H1, VVH1FR-H2, VVH1FR-H3 and VVH1FR-H4 are respectively shown as SEQ ID NOs. 4-7; and the complementary determining regions include VVH1CDR-H1, VVH1 CDR-H2 and VVH1 CDR-H3, and the amino acid sequences of VVH1 CDR-H1, VVH1 CDR-H2 and VVH1 CDR-H3 are respectively shown as SEQ ID NOs. 1-3. The nanobody has high binding activity with IL-23A, has the characteristics of small molecular weight, good stability, good tissue wettability, weak immunogenicity and the like compared with a traditional antibody, and can be applied to the preparation of an antibody drug targeting IL-23A so as to treat related diseases through combination with IL-23A.

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.

Provided herein are nanobodies, polypeptides comprising the same, and uses thereof. The nanobody's variable region includes 3 complementarity determining regions (CDRs) and framework regions (FRs), wherein the CDRs are as follows: CDR1: Ser-Gly-Xaa11-Xaa12-Phe-Xaa13-Xaa14-Asn-Xaa15 (Formula I); CDR2: Xaa21-Thr-Xaa22-Xaa23-Gly-Xaa24-Thr (Formula II); CDR3: His-Xaa31-Asp-Glu-Xaa32-Arg-Xaa33-Ser-Xaa34-Trp-Thr-Thr-Ser-Asn-Xaa35 (Formula III). The nanobodies and their polypeptides exhibit high affinity and activity, specifically recognizing and binding AAV. Affinity agents prepared therefrom have strong AAV adsorption capacity, suitable for AAV affinity chromatography to facilitate its industrial application. They are also applicable to AAV detection, enabling simultaneous detection of empty capsids and viral particles.

Disclosed are a nanobody targeting fibroblast activation protein-α, and the use thereof. An amino acid sequence of the nanobody comprises antigenic determinant complementary regions and framework regions with special structures. Firstly, alpacas are immunized with a recombinant FAPα antigen protein constructed to obtain a cell construct of alpaca PBMCs; secondly, an antibody targeting FAPα is screened by means of yeast display technology; and finally, an antibody having high sensitivity and specificity is obtained by means of functional detection and sequencing result analysis. The provided nanobody has the ability to specifically recognize and bind to FAPα, and has the characteristics of small molecular weight, low immunogenicity, better stability, a significant inhibitory effect on FAPα-expressing cells or tissues, etc., thus providing a potential therapeutic strategy for a disease involving FAPα expression. When the nanobody is used for developing or screening a diagnostic or therapeutic drug for FAPα-expressing cells or tissues, the obtained drug has excellent specificity and affinity, and has a significant inhibitory effect on FAPα-expressing cells or tissues.

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.

Provided are humanized framework region templates for the development of humanized antibodies. Further provided are the humanized anti-CD3ε antibodies. The humanized anti-CD3ε antibodies described herein are useful in methods for modulating an immune response.

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.

To provide improved methods for the production of heavy chain-only antibodies, which have less propensity for aggregation and retain high affinity for their intended target.SOLUTION: In one aspect, the present invention provides an isolated human or chimeric heavy chain-only antibody (HCAb) comprising a heavy chain variable (VH) domain, comprising complementarity determining regions (CDRs) and framework regions (FRs), having binding affinity to a target antigen in the absence of an antibody light chain, where in the VH domain the native amino acid residue at the first position of the fourth framework region (FR4) of the HCAb is substituted by a different amino acid residue that is capable of disrupting a surface-exposed hydrophobic patch comprising or associated with the native amino acid residue at that position.SELECTED DRAWING: Figure 1

The invention discloses an anti-CHMP4B nano antibody, the anti-CHMP4B nano antibody comprises a frame region FR and an antigenic determinant complementary region CDR, the antigenic determinant complementary region CDR comprises the following amino acid sequences: CDR1, CDR2 and CDR3: (1) CDR1-CDR3 of which the amino acid sequences are shown as SEQ ID NO.4, 7 and 10 in sequence, and (2) CDR1-CDR3 of which the amino acid sequences are shown as SEQ ID NO.3, SEQ ID NO.4, SEQ ID NO.7 and SEQ ID NO.10 in sequence; or (2) CDR1-CDR3 of which the amino acid sequences are shown as SEQ ID NO.5, 8 and 11 in sequence; or (3) CDR1-CDR3 of which the amino acid sequences are shown as SEQ ID NO.6, 9 and 12 in sequence. The nanomole-level high-affinity nano antibody aiming at CHMP4B is obtained through different amino acid sequences of FR and CDR regions, and the human or mouse CHMP4B protein can be specifically recognized.

The invention discloses a nanometer detection antibody targeting IL-23A and application thereof, and belongs to the field of biological medicines.The nanometer detection antibody is VHH2 and comprises a framework region and a complementarity determining region; the framework region comprises an FR-H1, an FR-H2, an FR-H3 and an FR-H4 of which the amino acid sequences are respectively shown as SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6 and SEQ ID NO: 7; by providing two high-affinity nano antibodies VHH2 and VHH3 with clear sequences, the technical problems of limited sensitivity, narrow application scene and the like caused by large molecular weight, poor permeability and poor stability of a traditional antibody in an existing IL-23A detection tool are solved; the precise detection effects of ultra-sensitivity and high specificity to the IL-23A and suitability for various detection platforms are achieved.

This invention belongs to the fields of molecular virology and immunology, and provides an alpaca-derived nanobody that specifically binds to Chikungunya virus (CHIKV), its preparation method, and its applications. The nanobody has a heavy chain variable region (VHH), which comprises the following CDRs: CDR1 (amino acid sequence as shown in SEQ ID NO:1), CDR2 (amino acid sequence as shown in SEQ ID NO:2), and CDR3 (amino acid sequence as shown in SEQ ID NO:3). The VHH includes four frame regions FR1-FR4; FR1, FR2, FR3, and FR4 are arranged alternately with CDR1, CDR2, and CDR3 in sequence. The nanobody of this invention can efficiently neutralize CHIKV virus and inhibit its infection, and has the potential to prepare drugs or kits for the prevention, treatment, and / or detection of CHIKV infection. The nanobody of this invention can bind with high affinity to the E protein of CHIKV, effectively inhibiting CHIKV pseudovirus infection.

The application discloses a bisphenol A monoclonal antibody and application thereof, and belongs to the technical field of biology. The monoclonal antibody contains a heavy chain variable region and a light chain variable region, the heavy chain variable region and the light chain variable region are both composed of a complementarity determining region and a framework region, and the complementarity determining region is composed of CDR1, CDR2 and CDR3. The monoclonal antibody can be used for preparing a bisphenol A detection product. The bisphenol A colloidal gold detection test strip provided by the application has the characteristics of high sensitivity, good specificity and strong stability.

To provide an antibody specifically binding to Axl protein, an immunoconjugate and a pharmaceutical composition.SOLUTION: Provided are single-chain antigen-binding antibodies that specifically bind to Axl proteins, comprising a heavy chain variable region and a light chain variable region having specific amino acid sequences, wherein all of the amino acid sequence mutations to the specific amino acid sequences occur only in the framework regions, and wherein the antibodies have higher binding affinities to Axl proteins at a pH of a tumor microenvironment ranging from pH7. 8 to 7.0 compared to a non-tumor microenvironment ranging from pH5. 2 to 7.6. Also provided is an immunoconjugate comprising the single-chain antigen-binding antibody, a linker molecule, and one or more cytotoxic agents covalently attached to the single-chain antigen-binding antibody and the linker molecule. Further provided is a pharmaceutical composition comprising said single-chain antigen-binding antibody for use as a medicament for the treatment of carcinoma.SELECTED DRAWING: None

The application discloses a kind of NbP1 single-domain antibody, TAT-NbP1 fusion single-domain antibody and purposes thereof, belong to biological medicine technical field.The NbP1 single-domain antibody of the application is used to specifically bind new coronavirus PLpro antigen, the NbP1 single-domain antibody is composed of framework region FR and three complementarity determining regions CDR1, CDR2 and CDR3;The amino acid sequence of CDR1 is as shown in SEQ ID NO.1, the amino acid sequence of CDR2 is as shown in SEQ ID NO.2, the amino acid sequence of CDR3 is as shown in SEQ ID NO.3.TAT-NbP1 fusion single-domain antibody is the fusion protein of NbP1 single-domain antibody and HIV-1 virus TAT peptide segment.The NbP1 single-domain antibody and TAT-NbP1 fusion single-domain antibody provided by the application have both antiviral and anti-inflammatory activities, and are safe, which provides a new idea for treating SARS-CoV-2 infection and developing anti-SARS-CoV-2 drugs.

The present disclosure provides a method of treating autoimmune diseases such as multiple sclerosis, comprising the use of anti-CD20 chimeric antigen receptor (CAR) that contains a hybrid single chain variable fragment (scFv), wherein the framework regions (FRs) and complementarity-determining regions (CDRs) of the scFv are derived from different anti-CD20 antigen binding regions or anti-CD20 antibodies. Furthermore, the CAR comprises a torsional linker (e.g. 1-4 alanine residues) between the transmembrane domain and the cytoplasmic region of the CAR.

The application relates to an anti-Bacillus cereus nanobody and application thereof, the nanobody comprising a framework region FR and a complementarity determining region CDR, wherein the complementarity determining region CDR is CDR1 with an amino acid sequence as shown in SEQ ID NO. 6, CDR2 with an amino acid sequence as shown in SEQ ID NO. 7 and CDR3 with an amino acid sequence as shown in SEQ ID NO. 8. The nanobody can recognize and combine with Bacillus cereus, and has the advantages of easy expression and high expression efficiency, so that the nanobody can be applied to an enzyme-linked immunoassay method for detecting Bacillus cereus.

The invention discloses a spiramycin monoclonal antibody and application thereof, and belongs to the technical field of biology. The monoclonal antibody contains a heavy chain variable region and a light chain variable region, the heavy chain variable region and the light chain variable region are both composed of complementary determining regions and frame regions, and the complementary determining regions are both composed of CDR1, CDR2 and CDR3. The monoclonal antibody can be used for preparing a spiramycin detection product. The spiramycin colloidal gold test strip provided by the invention has the characteristics of high sensitivity, good specificity and strong stability.

Provided herein are, inter alia, recombinant proteins and humanized antibodies (e.g., bispecific antibodies, chimeric antigen receptors and humanized antibodies), which bind Cluster of Differentiation 84 (CD84) with high efficiency and specificity. The compositions provided herein include novel light and heavy chain domain CDRs and framework regions and are, inter alia, useful for treating cancer and other CD84-related diseases.