19 results about "Histone H3" patented technology

The invention provides application of lactic acid modified histone H3 in preparation of drugs and / or diagnostic kits for preventing and / or treating pancreatic ductal adenocarcinoma, and belongs to the technical field of disease diagnosis and / or treatment. The invention provides application of a lactic acid modified histone H3 as a target spot in preparation of a pancreatic ductal adenocarcinoma diagnostic kit or a medicine for preventing and / or treating pancreatic ductal adenocarcinoma. The site of lactic acid modification is 23-site lysine. The expression of H3K23la detected in clinical sample tissues in pancreatic ductal adenocarcinoma tumor tissues is obviously higher than that in para-carcinoma normal tissues, overexpression and non-expression of H3K23la in cells are regulated and controlled through in-vitro experiments in combination with overexpression and knock-down technologies, and results show that proliferation, invasion and migration capacities of pancreatic ductal adenocarcinoma cells are remarkably inhibited, so that the pancreatic ductal adenocarcinoma cells are remarkably inhibited. Therefore, the H3K23la can be used as a target spot for diagnosis and treatment of the pancreatic duct adenocarcinoma, and has wide application in diagnosis or treatment of the pancreatic duct adenocarcinoma.

The application provides a histone modification marker combination for sepsis and application and kit thereof, and belongs to the field of biomarkers. Through obtaining peripheral blood mononuclear cells, histone extraction, Western blot detection and data analysis, it is proved that the ratio (H3K18la / ac) of the acetylation modification level (H3K18ac) and the lysine residue lactylation modification level (H3K18la) of the 18th lysine residue of histone H3 can be used as a sepsis evaluation marker, and the kit can be used for distinguishing sepsis infection severe cases from non-infection severe cases, sepsis severity evaluation and sepsis prognosis prediction.

The invention discloses application of a DNTTIP1 gene in preparation of acute leukemia treatment medicines, and belongs to the technical field of biological medicines. The problem of providing a new scheme for preparing acute leukemia treatment medicines is solved. The DNTTIP1 gene is used as a drug target of a biomarker, an inhibitor MS-275 of an interaction protein HDAC1 of the DNTTIP1 and a simulant ABT199 of a downstream target gene BMF are jointly applied to preparation of a drug for treating acute leukemia, and deletion of the interaction protein 1 gene DNTTIP1 at the tail end of deoxynucleotidyl transferase can damage recruitment of histone deacetylase 1 HDAC1 to chromatin. According to the present invention, with the application of the BMF promoter, the high acetylation of the histone H3 lysine 27 on the BMF promoter of the B cell lymphoma 2 modification factor is caused, the BMF is reactivated, and the reactivated BMF competitively destroys the BCL2 mediated survival pathway so as to trigger the coordinated autophagy and apoptosis;

The present invention relates to wheat plants comprising a mutation causing an alteration of the amino acid sequence in centromere histone H3 (CENH3), which have the biological activity of a haploid inducer. Further, the present invention provides methods of generating the wheat plants of the present invention and haploid and doubled haploid wheat plants obtainable by crossing the wheat plants of the present invention with wildtype wheat plants.

The invention discloses application of tazeostat in preparation of a medicine for preventing and treating cardiac transplantation chronic rejection, and belongs to the technical field of biological medicine. The medicine reduces the trimethylation level of histone H3 around a B cell p21 gene at a lysine 27 site through epigenetic regulation, relieves epigenetic inhibition on the p21 gene to highly express p21 molecules, influences differentiation of the B cell to a hair growth center B cell and plasma cells, and further relieves antibody-mediated rejection reaction, so that the survival time of a graft is remarkably prolonged, and the survival rate of the graft is improved. The function of the transplanted heart is improved.

The present invention provides the use of histone modification markers in the preparation of sepsis diagnostic products and a kit thereof, belonging to the field of biomarkers. By obtaining peripheral blood mononuclear cells, histone extraction, Western blot detection, and data analysis, the present invention demonstrates that the acetylation level of histone H3 lysine 18 residue (H3K18ac) can be used as a sepsis assessment marker. The reagent used to detect H3K18ac can be used to prepare a kit for distinguishing severe infections from non-severe infections, assessing sepsis severity, or predicting sepsis prognosis.

The present disclosure relates to anti-CitH3 (citrullinated histone H3) antibodies, antigen binding fragments and uses thereof.

The invention discloses application of a protein marker in preparation of a product for diagnosing AAA, a kit and a use method of the kit. The kit is high in sensitivity and specificity and has a good diagnosis effect. According to the application of the protein marker in preparation of a product for diagnosing AAA, the protein marker is any one of the following proteins or a combination of the following proteins: a fibrinogen alpha chain, a fibrinogen gamma chain, histone H3.1 and S100-P protein.

The application of DNTTIP1 gene in preparing acute leukemia treatment drugs belongs to the technical field of biological medicine, and provides a new solution to the preparation of acute leukemia treatment drugs. The present application uses DNTTIP1 gene as a biomarker drug target, and combines the inhibitor MS-275 of the interaction protein HDAC1 of DNTTIP1 and the downstream target gene BMF analog ABT199 to prepare acute leukemia treatment drugs. The deletion of deoxynucleotide transferase terminal interaction protein 1 gene DNTTIP1 will damage the recruitment of histone deacetylase 1 HDAC1 to chromatin, cause high acetylation of histone H3 lysine 27 on B-cell lymphoma 2 modifier factor BMF promoter, and re-activate BMF. The re-activated BMF competitively destroys the BCL2-mediated survival pathway, triggers coordinated autophagy and apoptosis.

The invention relates to methods and uses of cell free histone H3 isoforms H3.1, H13.2, H3t and / or H3.3 (or cell free nucleosomes containing said isoforms) of determining the origin of a cell free histone or cell free nucleosome in a body fluid sample as originating from a dividing or non-dividing cell.

The invention discloses a wheat character improvement and new germplasm creation method based on apparent modification change, which is characterized in that a gene H3K27M (the nucleotide sequence is as shown in SEQ ID NO.1, and the coded amino acid sequence is as shown in SEQ ID NO.2) obtained by mutating lysine (K) at the 27th site of rice histone H3 into methionine (M) is introduced into wheat Fielder, so that the modification level of a wheat whole genome H3K27me3 is reduced. Experiments prove that the wheat material obtained by the method can significantly improve the drought tolerance of wheat, improve the grain quality and increase the yield-related traits. The H3K27M gene and related biological materials thereof provided by the invention can be used for improving the yield, quality and drought tolerance of wheat, an efficient technical approach is provided for rapidly cultivating new germplasm of high-yield, high-quality and drought-tolerant wheat, and the H3K27M gene and related biological materials have important significance on guaranteeing grain safety, promoting wheat breeding technology upgrading and accelerating the breeding process.

The present invention provides an H3S28 phosphorylation inhibitor or a composition containing the same. [Solution] A histone H3 phosphorylation inhibitor comprising a benzaldehyde compound or a pharmaceutically acceptable salt thereof is provided. The inhibitor or a composition comprising the same can be used to prevent, treat, or treat various cancers involving the H3S28ph protein (e.g., hepatic cancer, pancreatic cancer, lung cancer, ovarian cancer, colon adenocarcinoma, chronic myeloid leukemia, pancreatic ductal adenocarcinoma, malignant kidney tumor, breast cancer, melanoma, etc.), radiation-resistant cancers of these cancers, heart failure, and their complications, or to treat poor prognoses, by inhibiting the expression of the H3S28ph protein. Preferably, the benzaldehyde compound is benzaldehyde, 5,6-O-benzylidene-L-ascorbic acid, monosodium 5,6-O-benzylidene-L-ascorbic acid, 4,6-O-benzylidene-D-glucopyranose, or N-benzylideneethylamine.

The invention discloses a histone H3 hypoacetylation mediated heart gene expression regulation method, and relates to the technical field of biological medicines. Comprising the following steps: inducing a low acetylation state of a specific site of histone H3 in heart tissue by applying a histone acetylation inhibitor so as to inhibit gene expression of embryo transcription factors GATA4 and MEF2C; the low acetylation status is directed against lysine sites of histone H3, including at least one of H3K4, H3K9, and H3K27. The accurate epigenetic regulation and control mechanism is different from the traditional gene knockout or overexpression technology, and the transcriptional activity of the key gene for embryonic heart development is accurately regulated and controlled by regulating histone acetyl under the condition that a DNA sequence is not changed.

The invention relates to immunotherapeutic treatment of cancer. In particular, the invention relates to methods of treating cancer carrying a histone H3 K27M (H3K27M) mutation (e.g., diffuse midline glioma with H3K27M mutation) using immunotherapeutic compositions comprising immune cells engineered to express GD2-specific chimeric antigen receptors.

The invention provides a histone combination, a histone antibody detection reagent, a kit and application of the histone combination, the histone combination comprises multiple histone proteins, the multiple histone proteins comprise histone H1, histone H2A, histone H2B, histone H3 and histone H4, the multiple histone proteins exist in the form of first polymers and / or in the form of free monomers, and the histone antibodies exist in the form of second polymers and / or in the form of free monomers. The fifth lysine of the histone H2A has acetylation modification; the fifth, twelfth, fifteenth and twenty sites of lysine of the histone H2B have acetylation modification; the 9th, 14th, 18th, 23rd, 56th, 64th and 122nd lysine of the histone H3 has acetylation modification, and the 27th lysine of the histone H3 has methylation modification; and the fifth, eighth, twelfth and sixteenth lysine of the histone H4 has acetylation modification. By utilizing the histone combination, the detection rate of the histone antibody can be effectively improved, so that the detection result is more accurate.

The present invention relates to a method of analyzing cancer comprising detecting or measuring the trimethylation (H3K27Me3) level of lysine 27 on histone H3 of cell-free nucleosomes in a bodily fluid sample obtained from a subject, as well as related uses and kits using said method.

The present invention relates to a method for analyzing cancer, comprising detecting or measuring the level of trimethylation of histone H3 lysine 27 (H3K27Me3) in cell-free nucleosomes in a body fluid sample obtained from a subject, as well as related uses and kits for using the method.

The application discloses an anti-histone modification antibody, a covalently coupled Tn5 complex and application thereof. The anti-histone modification antibody specifically binds to any one or a combination of at least two of the following histone modifications: (1) histone H3 lysine acetylation modification H3K27ac at the 27th position; (2) histone H3 lysine trimethylation H3K27me3 at the 27th position; (3) histone H3 lysine monomethylation H3K4me1 at the 4th position; and (4) histone H3 lysine trimethylation H3K4me3 at the 4th position. The application forms an in-vitro stable recombinant antibody-Tn5 covalent isopeptide bond through a Catcher-Tag system, completely eliminates cross contamination in multi-target detection, perfectly retains the activity of the anti-histone modification antibody and the transposase, and realizes high-fidelity, low-background joint detection of a multi-epigenetic regulation network.