76 results about "Humanin" patented technology

The invention belongs to the technical field of antibody preparation, and particularly relates to an anti-human carbohydrate antigen CA125 monoclonal antibody and application thereof. The amino acid sequences of CDR1-3 on a light chain variable region of the monoclonal antibody are respectively shown as SEQ ID NO.3-5, and the amino acid sequences of CDR1-3 on a heavy chain variable region of the monoclonal antibody are respectively shown as SEQ ID NO.8-10. The monoclonal antibody provided by the invention can specifically recognize and bind to a natural carbohydrate antigen CA125 expressed by human cells or tissues, has good affinity and relatively high sensitivity of binding of the antibody and the antigen, has strong anti-interference ability to complex non-target protein components in the cells / tissues, is beneficial to significantly improving the accuracy and reliability of immunodetection of human CA125 protein, and has good application prospects. The method is suitable for high-specificity, high-sensitivity and high-reliability detection of the human CA125 protein, and has good applicability in a plurality of detection systems such as immunoblotting, immunoprecipitation, immunohistochemistry and the like.

The invention discloses a fusion protein of a bispecific antibody targeting a T cell and Her2 in series connection with IL-15 and a receptor thereof and an application of the fusion protein. Belongs to the technical field of biology. The fusion protein disclosed by the invention can be combined with a recombinant human CD3 protein and a recombinant human Her2 protein, can be combined with NK92 and SK-BR-3 cell lines, can stimulate NK92 cell proliferation, and can respectively cause ADCC effects mediated by T and NK cells; the antibody has important economic and social significance.

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 invention belongs to the field of biological medicine, and particularly relates to a recombinant adenovirus and application thereof. The technical problem to be solved by the invention is to provide the recombinant adenovirus with good tumor inhibition effect and high efficiency. The technical scheme of the invention is a recombinant adenovirus. The recombinant adenovirus is a replication-defective adenovirus, and an exogenous nucleic acid fragment is operably inserted into a viral genome; the exogenous nucleic acid fragment is a coding gene of human p53 protein, a coding gene of GM-CSF and a coding gene of RGD. The coding gene of the human p53 protein, the coding gene of the GM-CSF and the coding gene of the RGD are jointly constructed into the replication-deficient adenovirus, so that the adenovirus with multiple advantages is obtained, the tumor cell killing efficiency is improved by 2-4 times compared with that before recombination, and a new effective choice is provided for tumor immunotherapy.

Compositions and methods for the treatment of retinal degeneration are provided. In one aspect, provided herein is adeno-associated virus (AAV) vector comprising an AAV capsid having encapsidated therein a vector genome comprising AAV inverted terminal repeat (ITR) sequences, a human protein kinase B (AKT) coding sequence, and expression control sequences that direct expression of AKT in a host cell.

The present application provides a monoclonal antibody targeting human carcinoembryonic antigen CEACAM5 / 6, and a bispecific antibody capable of simultaneously targeting human carcinoembryonic antigen CEACAM5 / 6 and human CD47, a preparation method and applications. Specifically, it relates to an anti-human CD47 antibody and antigen-binding fragments thereof capable of simultaneously (1) specifically binding to human CD47 protein and blocking its binding to SIRPalpha, thereby thus blocking the inhibitory effect of CD47 on SIRPalpha-expressing macrophages; (2) specifically binding to human carcinoembryonic protein CEACAM5 / 6. The present application also relates to a preparation method and uses of the bispecific antibody.

The application relates to the technical field of biological medicine, and provides an anti-GPC3 full humanization single-domain antibody and application thereof. The application uses phage display technology to obtain one anti-human GPC3 specificity full humanization monoclonal single-domain antibody through antibody screening by targeting human GPC3 protein. The obtained single-domain antibody can be specifically combined with human GPC3, and can effectively inhibit the nuclear translocation of YAP, provides an effective alternative antibody drug for GPC3-targeted HCC treatment, and has a potential clinical application prospect.

An anti-CCR8 antibody or antigen-binding fragment thereof. The anti-CCR8 antibody can recognize human CCR8 protein, block the signal pathway between CCR8 and CCL1 / CCL18, and recognize cells expressing CCR8, and also has target specific ADCC activity on target cells expressing CCR8.

The invention relates to the technical field of biological medicine, in particular to a specific antibody for detecting or targeting ALDOA-K13 succinylation modification and application of the specific antibody. The specific antibody for detecting or targeting ALDOA-K13 succinylation modification can be specifically combined with a succinylation modification site of 13th lysine of human ALDOA protein, and is not combined with ALDOA of an unmodified type or other modified types. The invention provides a specific antibody for detecting or targeting ALDOA-K13 succinylation modification for the first time, and fills the blank of existing detection tools. The antibody not only has high specificity and sensitivity, but also can be used for developing a novel tumor diagnosis and prognosis detection method.

Provided herein are bispecific and multispecific antibodies that target tumor antigens and 4-1BB, the Fc region of which has a retained or enhanced effector function; in particular, the multispecific antibodies have binding specificity for human ROR1 protein and human 4-1BB protein. Also provided herein are methods of treating cancer using the antibodies or fragments thereof.

The invention discloses a polypeptide targeting CD38, a ligand of the polypeptide, a coupling drug and application of the polypeptide, and the polypeptide targeting CD38 has an obvious binding signal with human CD38 protein, which shows that the polypeptide targeting CD38 has very high targeting property on CD38. A ligand or a coupling drug can be prepared from any sequence of the peptide targeting CD38, or a combination of a plurality of sequences, and an active drug is loaded or connected. The compound has a good killing result on cells such as MM.1 S, MOLP-8, HL-60, MV-4-11, Kasumi-1, K562 and KG-1, and has a relatively high growth inhibition rate on tumor cells such as a human multiple myeloma MOLP-8 cell strain and a human leukemia tumor cell HL-60 cell strain.

An in vitro method of detecting one or more endotoxins of one or more pathogens in a sample, comprising the steps of a. coating a lipid binding protein on a substrate or capturing a lipid binding protein on a capture molecule immobilized on a substrate, b. contacting the lipid binding protein, thus coated or captured, with the sample, c. detecting whether an endotoxin binds to the lipid binding protein, wherein the one or more endotoxins comprise a lipid A moiety and O- polysaccharide moiety, wherein the lipid binding protein is capable of binding the lipid A moiety of an endotoxin, and characterized in that the lipid binding protein is a mammalian protein and preferably is a murine or human protein.

Herein is reported an anti-TREM2 / A [beta] protein antibody comprising a first binding site that binds to human TREM2 and a second binding site that binds to human A [beta] protein, the first binding site comprising: a heavy chain variable domain comprising HVR-H1 of SEQ ID NO: 305, HVR-H2 of SEQ ID NO: 306 and HVR-H3 of SEQ ID NO: 307, and a light chain variable domain comprising HVR-L1 of SEQ ID NO: 309, HVR-L2 of SEQ ID NO: 310 and HVR-L3 of SEQ ID NO: 311 (TREM 23295), or a heavy chain variable domain comprising HVR-L1 of SEQ ID NO: 309, HVR-L2 of SEQ ID NO: 310 and HVR-L3 of SEQ ID NO: 311 (TREM 23295); the present invention relates to a single-chain variable domain comprising an HVR-H1 of SEQ ID NO: 329, an HVR-H2 of SEQ ID NO: 330, and an HVR-H3 of SEQ ID NO: 331, and a light chain variable domain comprising an HVR-L1 of SEQ ID NO: 333, an HVR-L2 of SEQ ID NO: 334, and an HVR-L3 of SEQ ID NO: 335 (TREM 23306); and a second binding site comprising: a heavy chain variable domain comprising HVR-H1 of SEQ ID NO: 09, HVR-H2 of SEQ ID NO: 10 and HVR-H3 of SEQ ID NO: 11, and in a light chain variable domain, HVR-L1 of SEQ ID NO: 13, HVR-L2 of SEQ ID NO: 14 and HVR-L3 of SEQ ID NO: 15 (A [beta] 8675).

Provided is an antibody for the treatment or prevention of autoimmune diseases, comprising a heavy chain variable region represented by SEQ ID NO: 1 or SEQ ID NO: 24, and a light chain variable region represented by SEQ ID NO: 6, SEQ ID NO: 11, SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, or SEQ ID NO: 25.

The present invention discloses a multifunctional recombinant antibody and its preparation method and application. The present invention not only provides a monoclonal antibody that can specifically recognize human HER3 protein, but also provides its humanized recombinant antibody, and further reconstructs on this basis to obtain a multifunctional antibody that can recognize human HER3 and has IL15 function, which can effectively enhance the killing effect of the original antibody on tumor cells. At the same time, the present invention also obtains a reconstructed specific HER3 monoclonal antibody-IL15 bifunctional molecule by introducing a mutated human IgG1 constant region, which can effectively reduce the toxicity of the antibody and improve safety. The antibody of the present invention can recognize HER3 protein in a variety of tumor cells, and then has a killing effect on a variety of tumor cells. At the same time, the reconstructed multifunctional recombinant antibody has the advantages of a short drug metabolism cycle, low toxicity and high safety, and has great application prospects.

The present disclosure provides antibodies or fragments thereof having binding specificity for human ROR1 protein. In various examples, the antibodies or fragments thereof comprise VH CDRs and VL CDRs, or variants thereof, as disclosed herein. The disclosure also provides methods of treating cancer using the antibodies or fragments thereof.

Genetically modified non-human animals comprising a humanized interleukin-15 (IL-15) gene. Cells, embryos, and non-human animals comprising a human IL-15 gene. Rodents that express humanized or human IL-15 protein.

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.

Provided are an anti-CD3 antibody and a use thereof. Specifically, the provided anti-CD3 antibody can specifically bind to human and monkey CD3 proteins, and has similar binding properties. In addition, the provided anti-CD3 antibody has excellent bioactivity on various human CD3E proteins (including hCD3E&D heterodimer, and the like), and has significantly improved safety. Also provided is a humanized anti-CD3 antibody. The humanized antibody has properties of low immunogenicity, high hydrophilicity, and high stability, and is suitable for drug development.

The invention belongs to the technical field of biology, and relates to a fully human anti-BCMA monoclonal antibody, a tandem antibody and application thereof. The invention provides an elutriation method of a BCMA protein monoclonal antibody, preparation of an IgG antibody and optimization of a series antibody of the IgG antibody. The scFv monoclonal antibody is composed of a light chain variable region VL, a heavy chain variable region VH and a human Fc fragment. The base sequence of the scFv monoclonal antibody is as shown in SEQ ID No.9, and the amino acid sequence of the scFv monoclonal antibody is as shown in SEQ ID No.23. The anti-human BCMA IgG antibody can specifically recognize and bind to human BCMA protein, and the binding activity of the anti-human BCMA IgG antibody is remarkably improved after the anti-human BCMA IgG antibody is expressed in a series scFv antibody form. The tandem antibody has a wide application prospect in detection of human BCMA protein and treatment of related target diseases, and a new idea is provided for development of antibody diagnostic reagents and drugs.

The present invention provides a non-human animal with humanized TGFBR2 gene and its construction method, a humanized TGFBR2 protein, a humanized TGFBR2 gene, a targeting vector for TGFBR2 gene, a cell with humanized TGFBR2 gene and its application in the biomedical field. The construction method includes introducing a nucleotide sequence encoding human TGFBR2 protein into the genome of a non-human animal by means of homologous recombination. The human or humanized TGFBR2 protein can be normally expressed in this animal, which can be used as an animal model for studying the signal mechanism of human TGFBR2, screening drugs for tumors and immune-related diseases, and has important application value for the research and development of new drugs targeting immune targets.

The application discloses application of recombinant human USP13 protein in preparation of a drug for treating diabetic cardiomyopathy, and belongs to the technical field of biological medicines.The application first proves that the expression of USP13 in myocardial tissue and serum is significantly reduced under the condition of diabetic cardiomyopathy (DCM); the recombinant human USP13 protein can obviously reduce the level of myocardial cell active oxygen, reduce the expression of NLRP3 inflammasome and active Caspase3 protein in a DCM in-vitro model induced by high sugar / palmitic acid; in a DCM mouse model injected with the recombinant human USP13 protein through a tail vein, myocardial cell apoptosis is inhibited, and the expression of NLRP3 inflammasome and the synthesis of TNF-alpha in the heart of the animal are reduced.USP13 is a human protein, has no obvious toxic side effects, is high in safety, is small in immunological rejection in theory, provides a new effective drug for the clinical treatment of DCM, and has important clinical application value and industrialization prospect.

Provided is an isolated antibody or antigen-binding fragment thereof that binds specifically to human CD-L1 protein, a nucleic acid molecule encoding the same, therapeutic compositions thereof, and their use to treat a PD-L1 related disease, such as a tumor which is PD-L1 positive.

Disclosed in the present invention are an EGFR x HER3 bispecific antibody-drug conjugate, a preparation method therefor, and use thereof. The structure of the antibody-drug conjugate is A-(L1-L2-L3-T)n, wherein A refers to an antibody; L1 refers to a coupling linker; L2 refers to x PEG spacers; L3 refers to an enzymatically cleavable or cleavable linker, or a non-cleavable linker; and T refers to an active small molecule. The antibody-drug conjugate provided in the present invention can bind to an HER3 protein of a human EGFR protein, has cytotoxicity to cancer cells expressing EGFR and / or HER3, and exhibits better efficacy and safety in in vivo tumor treatment.

The present disclosure provides an antibody or an antigen-binding fragment thereof, which specifically binds to PVRIG, has high binding affinity to human PVRIG protein and cynomolgus PVRIG protein, and has strong activity in both reporter gene level and CD8 T cell activation. Compared with known SRF813 and COM701, the antibodies of the present application exhibit more optimal in vitro activity, and some of the antibodies combined with PD-1 antibodies have obvious anti-tumor effect, making them excellent candidate drug molecules for therapeutic and diagnostic use.

The present disclosure provides a modified human OTC protein having improved properties for the treatment of OTC deficiency in a patient. Preferably, the protein of the disclosure is produced from a codon optimized mRNA suitable for administration to a patient suffering from OTC deficiency wherein upon administration of the mRNA to the patient, the protein of the disclosure is expressed in the patient in therapeutically effective amounts to treat OTC deficiency. The present disclosure also provides codon optimized mRNA sequences encoding wild type human OTC comprising a 5′ UTR derived from a gene expressed by Arabidopsis thaliana for use in treating OTC deficiency in a patient.

The present invention provides a nano - monoclonal antibody IDM2 - 27 targeting HER2, its preparation method and applications. The complementarity - determining regions (CDRs) of the nano - monoclonal antibody include CDR1, CDR2 and CDR3. Among them, the amino acid sequences of CDR1, CDR2 and CDR3 are GFTFSSYS, INSDGSST and GKGGLHYSDYE respectively. The nano - monoclonal antibody provided by the present invention has high specificity for human HER2 protein, strong affinity, is easy to produce and has high stability, and is suitable for various cancer diagnosis and treatment research targeting HER2.

The present disclosure provides compositions and methods for targeting neoantigens, for example, to treat or prevent cancer. Embodiments disclosed include binding proteins that bind to neoantigen:HLA complexes, such as T cell receptors. The binding proteins further include a fusion protein of a CD95 ectodomain and a CD137 intracellular signaling domain (Fas-41BB), and a construct comprising a CDS coreceptor α or β chain. The disclosed binding proteins are sensitive to antigens and can induce activation of host T cells with low concentrations of peptide antigens. In certain embodiments, the binding proteins of the present disclosure are (i) non-alloreactive, substantially non-alloreactive, and / or have a low risk of alloreactivity against amino acid sequences derived from the human proteome and / or (ii) human HLA alleles. Polynucleotides encoding such binding proteins can be introduced into host cells, such as T cells, and the cells can be used in immunotherapies for treating various cancers.

The present application relates to the field of physiology and molecular biology, and discloses an m 6 The present application relates to the field of physiology and molecular biology, and discloses an m 6 A binding protein IGF2BP3 ubiquitination and its application in preparation of an anti-tumor drug targeting RNA binding protein. Protein spectrum technology is used to screen the ubiquitination site of IGF2BP3, and the site mutation verifies that the ubiquitination site of IGF2BP3 is K213, which is located in the first KH domain of IGF2BP3. The functional analysis results show that after the mutation of IGF2BP3, the binding of IGF2BP3 with downstream tumor-related genes is weakened, the expression of the downstream tumor-related genes is down-regulated, and the growth of cervical cancer cells is inhibited, which indicates that ubiquitination modification is an important regulation mode affecting the function of IGF2BP3.

Herein is reported an antibody that binds to human A-beta protein wherein the antibody comprises a heavy chain variable domain (VH) and a light chain variable domain, the heavy chain variable domain and the light chain variable domain comprising a CDR selected from the group consisting of: (1) a CDR of SEQ ID NO: 85, 86, 87, 81, 82 and 83; or (2) a CDR of SEQ ID NO: 85, 89, 87, 81, 82, and 83; or (3) a CDR of SEQ ID NO: 85, 86, 87, 81, 82 and 91; or (4) CDRs of SEQ ID NO: 85, 89, 87, 81, 82 and 91.