358 results about "Complementarity determining region" patented technology

This invention discloses a monoclonal antibody against human hepatitis B e antigen and its application, relating to the field of hepatitis B detection technology. In the heavy chain variable region of the monoclonal antibody, the amino acid sequences of the complementarity-determining regions (CDR1-3) are as shown in SEQ ID NO. 1-3 or have at least 95% homology with the sequences shown in SEQ ID NO. 1-3; in the light chain variable region, the amino acid sequences of the complementarity-determining regions (CDR1 and CDR3) are as shown in SEQ ID NO. 4 and 5 or have at least 95% homology with the sequences shown in SEQ ID NO. 4 and 5, and the amino acid sequence of the complementarity-determining region (CDR2) is FAS. The monoclonal antibody provided by this invention can effectively recognize natural hepatitis B e antigen, and the titer of the supernatant from B cell culture can reach 1:10000, making it fully applicable to the detection and research of human hepatitis B e antigen. The chemiluminescent reagent prepared using the monoclonal antibody described in this invention has advantages such as high specificity, strong anti-interference ability, high detection sensitivity, and good stability, with almost no missed detections, and can replace imported reagents.

The invention relates to the field of biological detection, in particular to a monoclonal antibody combination for detecting human IL-6 protein and application. The combination comprises monoclonal antibodies 3A10 and 2G1, and amino acid sequences of complementary determining regions of variable regions of light and heavy chains of the monoclonal antibodies 3A10 and 2G1 are respectively shown as SEQ ID NO.1-12. The invention defines a complete variable region sequence and a coding nucleotide sequence of the antibody. The combination specifically recognizes human IL-6 recombinant and natural proteins, and has no cross reaction with IL-11. A double-antibody sandwich ELISA kit constructed based on the combination takes 3A10 as a coating antibody and 2G1 as a labeled antibody, and has high sensitivity and high specificity. The problems that an existing reagent is insufficient in specificity and low in sensitivity are solved, a reliable core raw material is provided for IL-6 standardized detection, and the method is suitable for preparation of a kit, a test strip and an antibody chip.

The invention provides a group of monoclonal antibody pairs targeting adenovirus DBP protein, the monoclonal antibody pairs comprise a capture antibody and a detection antibody, each of the two antibodies comprises a heavy chain variable region and a light chain variable region, the heavy chain variable region comprises heavy chain complementarity determining regions HCDR1, HCDR2 and HCDR3, the light chain variable region comprises light chain complementarity determining regions LCDR1, LCDR2 and LCDR3, and the capture antibody and the detection antibody are used for capturing and detecting the adenovirus DBP protein. Wherein the capture antibody is a monoclonal antibody 19E3; and the detection antibody is selected from a monoclonal antibody 96 to 10D8, a monoclonal antibody 95 to 2B7, a monoclonal antibody 96 to 2C10, a monoclonal antibody 96 to 8E10, a monoclonal antibody 96 to 13D5 or a monoclonal antibody 96 to 2B10. The monoclonal antibody pair disclosed by the invention can be used for efficiently detecting various types of HAdV DBP.

The invention relates to the technical fields of gene engineering, antibody engineering and immunodiagnosis. The invention provides a recombinant humanized anti-Cpn IgM monoclonal antibody. The monoclonal antibody comprises a light chain variable region and a heavy chain variable region, the light chain variable region comprises three complementary determining regions CDR1, CDR2 and CDR3, and the amino acid sequences of the three complementary determining regions are respectively shown as SEQ ID NO.3, SEQ ID NO.4 and SEQ ID NO.5; the heavy chain variable region comprises three complementary determining regions CDR1, CDR2 and CDR3, and the amino acid sequences of the three complementary determining regions are shown as SEQ ID NO.6, SEQ ID NO.7 and SEQ ID NO.8 respectively. The invention also provides a method for preparing the monoclonal antibody. The recombinant humanized anti-Cpn IgM monoclonal antibody provided by the invention is expressed in mammalian cells by utilizing a gene recombination technology, has the characteristics of high purity, small batch difference and the like, and can be applied to a Cpn IgM antibody detection kit as a quality control product; as a quality control product, the recombinant humanized anti-Cpn IgM monoclonal antibody has the advantages of high sensitivity, high safety, inter-batch stability and the like.

The present invention provides a rabies virus G protein antigen epitope targeting completely human monoclonal antibody and applications thereof, the completely human monoclonal antibody comprises a heavy chain variable region and a light chain variable region, the heavy chain variable region has three complementary determining region amino acid sequences: GDISSSCFY, IHYSGST and ARHRRGYCYDSEKGGTNWFDP, and the light chain variable region has three complementary determining region amino acid sequences: GDISSSCFY, IHYSGST and ARHRRGYCYDSEKGGTNWFDP. The amino acid sequences of the three complementary determining regions of the light chain variable region are respectively as follows: QGISND, ATS and LQDYEFPLT. The fully human monoclonal antibody has efficient and broad-spectrum anti-rabies virus neutralizing activity, is high in expression, fully human-derived and good in stability, and can be used for preparing rabies virus detection products or drugs for preventing and treating rabies.

The invention belongs to the technical field of biological detection, and particularly relates to a monoclonal antibody combination for detecting porcine epidemic diarrhea virus NP protein and application of the monoclonal antibody combination. The combination is composed of monoclonal antibodies 1E11 and 5C8 and can efficiently and specifically recognize porcine epidemic diarrhea virus NP protein, amino acid sequences of complementary determining regions of heavy chain and light chain variable regions of the combination are clear and are shown as SEQ ID NO.1-12 respectively, high specificity and high affinity of the antibodies are guaranteed, the antibody combination can effectively capture and detect target antigens, and the antibody combination can be used for detecting the porcine epidemic diarrhea virus NP protein. The risk of non-specific binding and cross reaction is reduced. The combination shows excellent sensitivity and specificity in detection platforms such as colloidal gold immunochromatography and the like, and provides a stable and reliable biological recognition tool for rapid and accurate detection of the porcine epidemic diarrhea virus.

The invention relates to the technical field of nano antibodies, in particular to an anti-FcRH5 nano antibody and application thereof. The invention provides an anti-FcRH5 nano antibody with high affinity and specificity, and the anti-FcRH5 nano antibody is based on a single-domain heavy chain variable region structure from camelidae and has the advantages of small molecular weight, high stability, strong tissue penetrability, easiness in engineering modification and the like. The nano antibody specifically recognizes and is combined with a high-expression and stable-expression target spot on the surface of a multiple myeloma cell through a complementary determining region of the nano antibody. The nano antibody disclosed by the invention can be used as a core recognition element for constructing various treatment or diagnosis tools such as chimeric antigen receptor T cells, bispecific antibodies, antibody drug conjugates or immunodetection probes and the like. According to the technical scheme, the technical problem that an anti-FcRH5 antibody with high quality and definite functionality is lacked in the prior art can be solved. The nano antibody provided by the invention has remarkable clinical transformation and industrialization advantages, and promotes multiple myeloma treatment to multi-target collaborative iteration.

The invention discloses a nano antibody of pre-F protein of a targeted respiratory syncytial virus and application of the nano antibody. The nano antibody comprises a heavy chain variable region, and the heavy chain variable region comprises heavy chain complementary determining regions CDR1, CDR2 and CDR3. The nano antibody disclosed by the invention can be specifically combined with RSV, and has a good application prospect in the aspect of RSV infection related diseases.

The present disclosure relates to anti-MSLN conjugates that include a binding agent, at least one linker attached to the binding agent; and at least one cytotoxic agent attached to the at least one linker. In some embodiments, the binding agent includes a heavy chain variable (VH) region and a light chain variable (VL) region, wherein the VH region includes a complementarity determining region HCDR1 sequence having the amino acid sequence set forth in SEQ ID NO:1, a HCDR2 having the amino acid sequence set forth in SEQ ID NO:2, and a HCDR3 having the amino acid sequence set forth in SEQ ID NO:3; and wherein the VL region includes a LCDR1 sequence having the amino acid sequence set forth in SEQ ID NO:4, a LCDR2 having the amino acid sequence set forth in SEQ ID NO:5, and a LCDR3 having the amino acid sequence set forth in SEQ ID NO:6. In some embodiments, the anti-MSLN conjugates may be used in methods of treating a MSLN+ cancer.

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 provides an anti-chlorpromazine monoclonal antibody and application and product thereof, and relates to the technical field of biology.The anti-chlorpromazine monoclonal antibody provided by the application has a variable region, which comprises a complementarity determining region CDR1-VH with an amino acid sequence as shown in SEQ ID NO.1, a complementarity determining region CDR2-VH with an amino acid sequence as shown in SEQ ID NO.2, a complementarity determining region CDR3-VH with an amino acid sequence as shown in SEQ ID NO.3, a complementarity determining region CDR1-VL with an amino acid sequence as shown in SEQ ID NO.4, a complementarity determining region CDR2-VL with an amino acid sequence as shown in SEQ ID NO.5 and a complementarity determining region CDR3-VL with an amino acid sequence as shown in SEQ ID NO.6.The antibody has good specific binding capacity for chlorpromazine.

A conditionally active bispecific antibody comprising: an IgG antibody or antibody fragment that binds to human EpCAM protein, the IgG antibody or antibody fragment comprising a light chain variable region having three complementarity-determining regions L1, L2, and L3, and a heavy chain variable region having three complementarity-determining regions H1, H2, and H3; and at least one scFv antibody fragment that binds to a T lymphocyte protein linked to the C-terminus of at least one light chain of the IgG antibody or antibody fragment.

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 a preparation method and application of an anti-human CD20 nano antibody and a bivalent nano antibody, and belongs to the technical field of nano antibodies. The anti-human CD20 nano antibody or the antigen binding fragment thereof provided by the invention comprises three complementary determining regions CDR1, CDR2 and CDR3, the amino acid sequence of the CDR1 is the 26th to 33rd sites of SEQ ID NO: 1, the amino acid sequence of the CDR2 is the 51st to 57th sites of SEQ ID NO: 1, and the amino acid sequence of the CDR3 is the 96th to 110th sites of SEQ ID NO: 1. Experiments show that the conjugates are coupled with gamma delta T cells to specifically kill CD20 positive tumor cells, the possibility of medicine formation is achieved, and a new direction is provided for treatment of CD20 target spots.

The patent discloses an antibody against human IgG, a preparation method and application thereof, a heavy chain variable region of the antibody comprises heavy chain complementarity determining regions HCDR1, HCDR2 and HCDR3, and amino acid sequences are respectively shown as SEQ ID NO:1-3; a light chain variable region comprises light chain complementarity determining regions LCDR1, LCDR2 and LCDR3, and amino acid sequences are respectively shown as SEQ ID NO:4-6. The application efficiently prepares a high-activity monoclonal antibody which can combine with different subtypes of human IgG Fc by using an in-vitro culture method of B cells, and specifically relates to two monoclonal antibodies which can specifically combine with human IgG1 protein, and provides a powerful tool for detecting human IgG1 protein and researching diseases related to human IgG1 protein.

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.

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.

The application discloses a kind of nanobody for inhibiting bundibugio and zaire type Ebola virus infection.The application belongs to the field of biotechnology, specifically relates to a kind of nanobody for inhibiting bundibugio and zaire type Ebola virus infection.The nanobody BDBV-Nb02 of the application targeted Ebola virus has three complementarity determining regions CDR1, CDR2 and CDR3;The amino acid sequence of CDR1 is the 27-33 of SEQ ID No:1, the amino acid sequence of CDR2 is the 47-58 of SEQ ID No:1, and the amino acid sequence of CDR3 is the 97-109 of SEQ ID No:1.Nanobody BDBV-Nb02 presents neutralization effect to bundibugio Ebola virus and zaire type Ebola virus, and has important application prospect and innovation significance in medical field.

This invention provides an antibody that binds to the Frizzled receptor, particularly an antibody that binds to the Frizzled receptor 4-cysteine-rich domain, and a method for using the same. [Solution] The present invention provides an isolated antibody and immunoconjugate that specifically bind to the Frizzled receptor (FZD) 4 cysteine-rich domain (CRD), comprising a light chain variable region and a heavy chain variable region, wherein the heavy chain variable region comprises complementarity-determining regions CDR-H1, CDR-H2, and CDR-H3, and the light chain variable region comprises complementarity-determining regions CDR-L1, CDR-L2, and CDR-L3, and the amino acid sequence of the CDR comprises or consists of a sequence selected from a specific group of sequences.

Immunoglobulin complementarity determining regions ("CDRs"), and immunoglobulin binding domains comprising those CDRs, that bind human lymphocyte antigen 6 family member G6D (LY6G6D), and their use for the preparation of LY6G6D-binding proteins finding use as immunotherapeutics.

The invention belongs to the technical field of immunodetection, and discloses a VB12 sandwich method antibody mAb10 or an antigen binding fragment thereof, and a preparation method and application thereof. The VB12 sandwich method antibody mAb10 or the antigen binding fragment thereof provided by the invention comprises a light chain variable region and a heavy chain variable region, the light chain variable region comprises complementary determining regions LCDR1, LCDR2 and LCDR3, and the heavy chain variable region comprises complementary determining regions HCDR1, HCDR2 and HCDR3. When the VB12 sandwich method antibody mAb10 is used for detecting a VB12 standard antigen, the detection sensitivity is lower than 0.02 ng / mL, a clinical sample is detected through a magnetochemiluminescence method, the correlation with R clinical comparison is good in the sample range of 0-2 ng / mL, and the VB12 sandwich method antibody mAb10 has important significance in the field of diagnosis and treatment of VB12 deficiency related 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 invention relates to a nano antibody for specifically recognizing a tacrolimus-antibody compound and application of the nano antibody, and belongs to the technical field of biological detection. A variable region of the nano antibody has three complementary determining regions CDR1, CDR2 and CDR3, can specifically recognize a tacrolimus-antibody compound, and can be used for detecting drugs by a double-antibody sandwich method; the kit is widely suitable for various immunodetection technologies such as an enzyme-linked immunosorbent assay (ELISA), a chemiluminescence immunoassay (CLIA), an electrochemical luminescence immunoassay (ECLIA), a fluorescence immunoassay (FIA), an immunochromatography test strip method and the like. According to the method, the limitation of a traditional competition method is overcome, high-sensitivity, high-specificity and high-stability detection is realized, the method can be adapted to various detection platforms, and a portable pretreatment process without centrifugation can also be realized.

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.

The invention discloses an antibody or an antigen binding fragment specifically binding to trop2. The antibody or the antigen binding fragment comprises heavy chain complementarity determining regions HCDR1, HCDR2 and HCDR3, and light chain complementarity determining regions LCDR1, LCDR2 and LCDR3, the amino acid sequence of the HCDR1 is as shown in SEQ ID NO.1, the amino acid sequence of the HCDR2 is as shown in SEQ ID NO.2, the amino acid sequence of the HCDR3 is as shown in SEQ ID NO.3, the amino acid sequence of the LCDR1 is as shown in SEQ ID NO.4, the amino acid sequence of the LCDR2 is as shown in SEQ ID NO.5, and the amino acid sequence of the LCDR3 is as shown in SEQ ID NO.6. The expression condition of trop2 in human breast cancer and pancreatic cancer cell membrane tissue samples can be detected through an immunohistochemical method, and the adjoint diagnostic kit for the humanized trop2 antibody coupling medicine has the advantages of assisting in precise medication and avoiding invalid treatment.