UA78526C2 - Antibody against caspase-8, a process for preparation and use of said antibody for development of elisa-analysis - Google Patents
Antibody against caspase-8, a process for preparation and use of said antibody for development of elisa-analysis Download PDFInfo
- Publication number
- UA78526C2 UA78526C2 UA2004042509A UA2004042509A UA78526C2 UA 78526 C2 UA78526 C2 UA 78526C2 UA 2004042509 A UA2004042509 A UA 2004042509A UA 2004042509 A UA2004042509 A UA 2004042509A UA 78526 C2 UA78526 C2 UA 78526C2
- Authority
- UA
- Ukraine
- Prior art keywords
- caspase
- antibody
- peptide
- antibodies
- protein
- Prior art date
Links
- 102000004091 Caspase-8 Human genes 0.000 title claims abstract description 197
- 108090000538 Caspase-8 Proteins 0.000 title claims abstract description 195
- 238000000034 method Methods 0.000 title claims abstract description 42
- 238000011161 development Methods 0.000 title claims abstract description 6
- 238000002360 preparation method Methods 0.000 title abstract description 6
- 230000008569 process Effects 0.000 title abstract description 6
- 238000002965 ELISA Methods 0.000 title abstract description 4
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 114
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 106
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 95
- 102000011727 Caspases Human genes 0.000 claims abstract description 57
- 108010076667 Caspases Proteins 0.000 claims abstract description 57
- 230000003053 immunization Effects 0.000 claims abstract description 43
- 238000002649 immunization Methods 0.000 claims abstract description 42
- 241001465754 Metazoa Species 0.000 claims abstract description 17
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 9
- 238000010828 elution Methods 0.000 claims abstract description 9
- 239000012634 fragment Substances 0.000 claims description 42
- 238000004458 analytical method Methods 0.000 claims description 14
- 238000012545 processing Methods 0.000 claims description 8
- 238000000749 co-immunoprecipitation Methods 0.000 claims description 7
- 108060003951 Immunoglobulin Proteins 0.000 claims description 6
- 102000018358 immunoglobulin Human genes 0.000 claims description 6
- 238000005406 washing Methods 0.000 claims description 6
- 239000000284 extract Substances 0.000 claims description 5
- 230000002163 immunogen Effects 0.000 claims description 5
- 210000001124 body fluid Anatomy 0.000 claims 1
- 239000010839 body fluid Substances 0.000 claims 1
- 238000000605 extraction Methods 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 abstract description 98
- 239000012133 immunoprecipitate Substances 0.000 abstract description 11
- 238000004140 cleaning Methods 0.000 abstract description 2
- FFGPTBGBLSHEPO-UHFFFAOYSA-N carbamazepine Chemical compound C1=CC2=CC=CC=C2N(C(=O)N)C2=CC=CC=C21 FFGPTBGBLSHEPO-UHFFFAOYSA-N 0.000 abstract 1
- 230000002860 competitive effect Effects 0.000 abstract 1
- 229940089063 epitol Drugs 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 description 78
- 102000005962 receptors Human genes 0.000 description 39
- 108020003175 receptors Proteins 0.000 description 39
- 238000001114 immunoprecipitation Methods 0.000 description 34
- 230000027455 binding Effects 0.000 description 26
- 241000699670 Mus sp. Species 0.000 description 25
- 238000009739 binding Methods 0.000 description 25
- 239000003446 ligand Substances 0.000 description 24
- 239000006166 lysate Substances 0.000 description 23
- 102000004196 processed proteins & peptides Human genes 0.000 description 23
- 230000000694 effects Effects 0.000 description 21
- 230000000638 stimulation Effects 0.000 description 21
- 239000000427 antigen Substances 0.000 description 19
- 239000013592 cell lysate Substances 0.000 description 19
- 238000003776 cleavage reaction Methods 0.000 description 19
- 230000007017 scission Effects 0.000 description 19
- 102000036639 antigens Human genes 0.000 description 18
- 108091007433 antigens Proteins 0.000 description 18
- 241000699666 Mus <mouse, genus> Species 0.000 description 16
- 230000006907 apoptotic process Effects 0.000 description 15
- 238000001262 western blot Methods 0.000 description 15
- 230000003834 intracellular effect Effects 0.000 description 14
- 235000001014 amino acid Nutrition 0.000 description 13
- 238000011534 incubation Methods 0.000 description 13
- 239000007787 solid Substances 0.000 description 13
- 230000004913 activation Effects 0.000 description 12
- 229940024606 amino acid Drugs 0.000 description 11
- 150000001413 amino acids Chemical class 0.000 description 11
- 239000002299 complementary DNA Substances 0.000 description 11
- 230000004927 fusion Effects 0.000 description 11
- 210000004408 hybridoma Anatomy 0.000 description 11
- 239000002773 nucleotide Substances 0.000 description 11
- 125000003729 nucleotide group Chemical group 0.000 description 11
- 230000015572 biosynthetic process Effects 0.000 description 10
- 238000000746 purification Methods 0.000 description 10
- 102000004190 Enzymes Human genes 0.000 description 9
- 108090000790 Enzymes Proteins 0.000 description 9
- 102000035195 Peptidases Human genes 0.000 description 9
- 108091005804 Peptidases Proteins 0.000 description 9
- 239000004365 Protease Substances 0.000 description 9
- 229940088598 enzyme Drugs 0.000 description 9
- 238000003752 polymerase chain reaction Methods 0.000 description 9
- 239000006228 supernatant Substances 0.000 description 9
- 238000004519 manufacturing process Methods 0.000 description 8
- 210000002966 serum Anatomy 0.000 description 8
- 230000008054 signal transmission Effects 0.000 description 8
- 239000007790 solid phase Substances 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 210000004899 c-terminal region Anatomy 0.000 description 7
- 238000006243 chemical reaction Methods 0.000 description 7
- 230000006870 function Effects 0.000 description 7
- 230000014509 gene expression Effects 0.000 description 7
- 102000034356 gene-regulatory proteins Human genes 0.000 description 7
- 108091006104 gene-regulatory proteins Proteins 0.000 description 7
- 230000002441 reversible effect Effects 0.000 description 7
- 239000000523 sample Substances 0.000 description 7
- 230000019491 signal transduction Effects 0.000 description 7
- 239000000758 substrate Substances 0.000 description 7
- 208000002109 Argyria Diseases 0.000 description 6
- 108090000572 Caspase-10 Proteins 0.000 description 6
- 102000004068 Caspase-10 Human genes 0.000 description 6
- 229920002684 Sepharose Polymers 0.000 description 6
- 230000030833 cell death Effects 0.000 description 6
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 6
- 150000001875 compounds Chemical class 0.000 description 6
- 238000001514 detection method Methods 0.000 description 6
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 6
- 230000001404 mediated effect Effects 0.000 description 6
- 235000019419 proteases Nutrition 0.000 description 6
- 102100027617 DNA/RNA-binding protein KIN17 Human genes 0.000 description 5
- 101000983528 Homo sapiens Caspase-8 Proteins 0.000 description 5
- 241000283973 Oryctolagus cuniculus Species 0.000 description 5
- 102000001708 Protein Isoforms Human genes 0.000 description 5
- 108010029485 Protein Isoforms Proteins 0.000 description 5
- 239000002671 adjuvant Substances 0.000 description 5
- 239000000872 buffer Substances 0.000 description 5
- 201000010099 disease Diseases 0.000 description 5
- 102000048448 human CASP8 Human genes 0.000 description 5
- 238000003018 immunoassay Methods 0.000 description 5
- 239000003112 inhibitor Substances 0.000 description 5
- 230000000977 initiatory effect Effects 0.000 description 5
- 230000003993 interaction Effects 0.000 description 5
- 210000001165 lymph node Anatomy 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 210000000952 spleen Anatomy 0.000 description 5
- 206010003445 Ascites Diseases 0.000 description 4
- 102000010170 Death domains Human genes 0.000 description 4
- 108050001718 Death domains Proteins 0.000 description 4
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 4
- 102100026933 Myelin-associated neurite-outgrowth inhibitor Human genes 0.000 description 4
- 229920001213 Polysorbate 20 Polymers 0.000 description 4
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 4
- 230000009471 action Effects 0.000 description 4
- 125000000539 amino acid group Chemical group 0.000 description 4
- 230000001413 cellular effect Effects 0.000 description 4
- 238000000975 co-precipitation Methods 0.000 description 4
- 235000018417 cysteine Nutrition 0.000 description 4
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 4
- 230000034994 death Effects 0.000 description 4
- 102000037865 fusion proteins Human genes 0.000 description 4
- 108020001507 fusion proteins Proteins 0.000 description 4
- 239000000499 gel Substances 0.000 description 4
- 239000008187 granular material Substances 0.000 description 4
- 238000002347 injection Methods 0.000 description 4
- 239000007924 injection Substances 0.000 description 4
- 238000002955 isolation Methods 0.000 description 4
- 239000007788 liquid Substances 0.000 description 4
- 239000012528 membrane Substances 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 239000013642 negative control Substances 0.000 description 4
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 4
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 4
- 239000002243 precursor Substances 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- -1 protocols Substances 0.000 description 4
- 238000011084 recovery Methods 0.000 description 4
- 210000001995 reticulocyte Anatomy 0.000 description 4
- 238000006467 substitution reaction Methods 0.000 description 4
- 238000011282 treatment Methods 0.000 description 4
- 210000004881 tumor cell Anatomy 0.000 description 4
- 102000001483 Initiator Caspases Human genes 0.000 description 3
- 108010054031 Initiator Caspases Proteins 0.000 description 3
- 241001529936 Murinae Species 0.000 description 3
- 206010028851 Necrosis Diseases 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 206010035226 Plasma cell myeloma Diseases 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- 210000001744 T-lymphocyte Anatomy 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 210000003719 b-lymphocyte Anatomy 0.000 description 3
- 230000001086 cytosolic effect Effects 0.000 description 3
- 230000001472 cytotoxic effect Effects 0.000 description 3
- 230000003013 cytotoxicity Effects 0.000 description 3
- 231100000135 cytotoxicity Toxicity 0.000 description 3
- 238000012217 deletion Methods 0.000 description 3
- 230000037430 deletion Effects 0.000 description 3
- 230000018109 developmental process Effects 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 3
- 230000006698 induction Effects 0.000 description 3
- 201000000050 myeloid neoplasm Diseases 0.000 description 3
- 230000017074 necrotic cell death Effects 0.000 description 3
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 3
- 239000002244 precipitate Substances 0.000 description 3
- 238000004007 reversed phase HPLC Methods 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- 102000003390 tumor necrosis factor Human genes 0.000 description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 208000023275 Autoimmune disease Diseases 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 102000014914 Carrier Proteins Human genes 0.000 description 2
- 108090000397 Caspase 3 Proteins 0.000 description 2
- 102100029855 Caspase-3 Human genes 0.000 description 2
- 102000004127 Cytokines Human genes 0.000 description 2
- 108090000695 Cytokines Proteins 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- 102000009058 Death Domain Receptors Human genes 0.000 description 2
- 108010049207 Death Domain Receptors Proteins 0.000 description 2
- 102000007989 Effector Caspases Human genes 0.000 description 2
- 108010089510 Effector Caspases Proteins 0.000 description 2
- 102000004878 Gelsolin Human genes 0.000 description 2
- 108090001064 Gelsolin Proteins 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 2
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- 108010067902 Peptide Library Proteins 0.000 description 2
- 239000004793 Polystyrene Substances 0.000 description 2
- 102100021409 Probable ATP-dependent RNA helicase DDX17 Human genes 0.000 description 2
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 101800000958 Reverse transcriptase/ribonuclease H Proteins 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 102000004142 Trypsin Human genes 0.000 description 2
- 108090000631 Trypsin Proteins 0.000 description 2
- 230000002776 aggregation Effects 0.000 description 2
- 238000004220 aggregation Methods 0.000 description 2
- 230000000890 antigenic effect Effects 0.000 description 2
- 230000001640 apoptogenic effect Effects 0.000 description 2
- 238000003782 apoptosis assay Methods 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 235000003704 aspartic acid Nutrition 0.000 description 2
- 239000011324 bead Substances 0.000 description 2
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 2
- 108091008324 binding proteins Proteins 0.000 description 2
- 230000008827 biological function Effects 0.000 description 2
- 230000033228 biological regulation Effects 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 239000012636 effector Substances 0.000 description 2
- 230000008030 elimination Effects 0.000 description 2
- 238000003379 elimination reaction Methods 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- 230000009931 harmful effect Effects 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 230000005847 immunogenicity Effects 0.000 description 2
- 238000003364 immunohistochemistry Methods 0.000 description 2
- 238000013198 immunometric assay Methods 0.000 description 2
- 230000001965 increasing effect Effects 0.000 description 2
- 230000006882 induction of apoptosis Effects 0.000 description 2
- 230000001939 inductive effect Effects 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 238000002372 labelling Methods 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 238000004020 luminiscence type Methods 0.000 description 2
- 210000004698 lymphocyte Anatomy 0.000 description 2
- 230000002934 lysing effect Effects 0.000 description 2
- 230000003211 malignant effect Effects 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 230000037353 metabolic pathway Effects 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- 150000002739 metals Chemical class 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 230000000869 mutational effect Effects 0.000 description 2
- 230000001338 necrotic effect Effects 0.000 description 2
- 108020004707 nucleic acids Proteins 0.000 description 2
- 102000039446 nucleic acids Human genes 0.000 description 2
- 150000007523 nucleic acids Chemical class 0.000 description 2
- 230000002018 overexpression Effects 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 229920002223 polystyrene Polymers 0.000 description 2
- 230000005522 programmed cell death Effects 0.000 description 2
- 230000000770 proinflammatory effect Effects 0.000 description 2
- 230000004850 protein–protein interaction Effects 0.000 description 2
- 230000002285 radioactive effect Effects 0.000 description 2
- 238000003127 radioimmunoassay Methods 0.000 description 2
- 230000008707 rearrangement Effects 0.000 description 2
- 230000000284 resting effect Effects 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 238000004611 spectroscopical analysis Methods 0.000 description 2
- 238000010186 staining Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 201000000596 systemic lupus erythematosus Diseases 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 239000012588 trypsin Substances 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 description 1
- HUDPLKWXRLNSPC-UHFFFAOYSA-N 4-aminophthalhydrazide Chemical compound O=C1NNC(=O)C=2C1=CC(N)=CC=2 HUDPLKWXRLNSPC-UHFFFAOYSA-N 0.000 description 1
- 108010072306 ATSO Proteins 0.000 description 1
- 102000012440 Acetylcholinesterase Human genes 0.000 description 1
- 108010022752 Acetylcholinesterase Proteins 0.000 description 1
- 102000007469 Actins Human genes 0.000 description 1
- 108010085238 Actins Proteins 0.000 description 1
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 1
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 108010024976 Asparaginase Proteins 0.000 description 1
- 102000015790 Asparaginase Human genes 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 208000011691 Burkitt lymphomas Diseases 0.000 description 1
- 206010006895 Cachexia Diseases 0.000 description 1
- 101100457021 Caenorhabditis elegans mag-1 gene Proteins 0.000 description 1
- 101100346155 Caenorhabditis elegans oma-2 gene Proteins 0.000 description 1
- 229940123169 Caspase inhibitor Drugs 0.000 description 1
- 102000004046 Caspase-2 Human genes 0.000 description 1
- 108090000552 Caspase-2 Proteins 0.000 description 1
- 102100035882 Catalase Human genes 0.000 description 1
- 108010053835 Catalase Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 102000005927 Cysteine Proteases Human genes 0.000 description 1
- 108010005843 Cysteine Proteases Proteins 0.000 description 1
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 description 1
- 102000036292 Death effector domains Human genes 0.000 description 1
- 108091010866 Death effector domains Proteins 0.000 description 1
- CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 description 1
- 101710088194 Dehydrogenase Proteins 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 102000010911 Enzyme Precursors Human genes 0.000 description 1
- 108010062466 Enzyme Precursors Proteins 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 241000237858 Gastropoda Species 0.000 description 1
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 description 1
- 102100022624 Glucoamylase Human genes 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 102000000587 Glycerolphosphate Dehydrogenase Human genes 0.000 description 1
- 108010041921 Glycerolphosphate Dehydrogenase Proteins 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 101000636168 Grapevine leafroll-associated virus 3 (isolate United States/NY1) Movement protein p5 Proteins 0.000 description 1
- 102000001554 Hemoglobins Human genes 0.000 description 1
- 108010054147 Hemoglobins Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000740484 Homo sapiens Aryl hydrocarbon receptor nuclear translocator-like protein 1 Proteins 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 102000004195 Isomerases Human genes 0.000 description 1
- 108090000769 Isomerases Proteins 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 description 1
- 108010047357 Luminescent Proteins Proteins 0.000 description 1
- 102000006830 Luminescent Proteins Human genes 0.000 description 1
- 102000008072 Lymphokines Human genes 0.000 description 1
- 108010074338 Lymphokines Proteins 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- 102000004083 Lymphotoxin-alpha Human genes 0.000 description 1
- 108090000542 Lymphotoxin-alpha Proteins 0.000 description 1
- 102000013460 Malate Dehydrogenase Human genes 0.000 description 1
- 108010026217 Malate Dehydrogenase Proteins 0.000 description 1
- 101710175625 Maltose/maltodextrin-binding periplasmic protein Proteins 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 108010059724 Micrococcal Nuclease Proteins 0.000 description 1
- 108090000143 Mouse Proteins Proteins 0.000 description 1
- 101000983527 Mus musculus Caspase-8 Proteins 0.000 description 1
- 101100067996 Mus musculus Gbp1 gene Proteins 0.000 description 1
- 101100018424 Mus musculus Ids gene Proteins 0.000 description 1
- 101100460719 Mus musculus Noto gene Proteins 0.000 description 1
- 101100478278 Mus musculus Spta1 gene Proteins 0.000 description 1
- 235000009421 Myristica fragrans Nutrition 0.000 description 1
- QPCDCPDFJACHGM-UHFFFAOYSA-N N,N-bis{2-[bis(carboxymethyl)amino]ethyl}glycine Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(=O)O)CCN(CC(O)=O)CC(O)=O QPCDCPDFJACHGM-UHFFFAOYSA-N 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 102000016979 Other receptors Human genes 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 239000004698 Polyethylene Substances 0.000 description 1
- 239000004743 Polypropylene Substances 0.000 description 1
- 101000983524 Rattus norvegicus Caspase-8 Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 206010040070 Septic Shock Diseases 0.000 description 1
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 1
- 102100024483 Sororin Human genes 0.000 description 1
- 101710172711 Structural protein Proteins 0.000 description 1
- 101710097834 Thiol protease Proteins 0.000 description 1
- 108700019146 Transgenes Proteins 0.000 description 1
- 102000005924 Triose-Phosphate Isomerase Human genes 0.000 description 1
- 108700015934 Triose-phosphate isomerases Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- 108010046334 Urease Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 101100187345 Xenopus laevis noto gene Proteins 0.000 description 1
- 229940022698 acetylcholinesterase Drugs 0.000 description 1
- DZBUGLKDJFMEHC-UHFFFAOYSA-N acridine Chemical class C1=CC=CC2=CC3=CC=CC=C3N=C21 DZBUGLKDJFMEHC-UHFFFAOYSA-N 0.000 description 1
- 210000001789 adipocyte Anatomy 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 230000009824 affinity maturation Effects 0.000 description 1
- 230000007720 allelic exclusion Effects 0.000 description 1
- 108010004469 allophycocyanin Proteins 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 229940025131 amylases Drugs 0.000 description 1
- 208000022531 anorexia Diseases 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 229960005475 antiinfective agent Drugs 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 210000003567 ascitic fluid Anatomy 0.000 description 1
- 229960003272 asparaginase Drugs 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-M asparaginate Chemical compound [O-]C(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-M 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 239000012472 biological sample Substances 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 238000005415 bioluminescence Methods 0.000 description 1
- 230000029918 bioluminescence Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 102000022254 caspase binding proteins Human genes 0.000 description 1
- 108091012122 caspase binding proteins Proteins 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 230000011748 cell maturation Effects 0.000 description 1
- 230000005889 cellular cytotoxicity Effects 0.000 description 1
- 230000007248 cellular mechanism Effects 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 235000010980 cellulose Nutrition 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003593 chromogenic compound Substances 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 238000005352 clarification Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000004737 colorimetric analysis Methods 0.000 description 1
- 238000004891 communication Methods 0.000 description 1
- 108091036078 conserved sequence Proteins 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 201000003740 cowpox Diseases 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 1
- 206010061428 decreased appetite Diseases 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000007123 defense Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000001066 destructive effect Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 230000002900 effect on cell Effects 0.000 description 1
- 239000012149 elution buffer Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- ZFKJVJIDPQDDFY-UHFFFAOYSA-N fluorescamine Chemical compound C12=CC=CC=C2C(=O)OC1(C1=O)OC=C1C1=CC=CC=C1 ZFKJVJIDPQDDFY-UHFFFAOYSA-N 0.000 description 1
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- 210000003714 granulocyte Anatomy 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 108060003552 hemocyanin Proteins 0.000 description 1
- 206010019692 hepatic necrosis Diseases 0.000 description 1
- 239000000833 heterodimer Substances 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 235000003642 hunger Nutrition 0.000 description 1
- 210000004754 hybrid cell Anatomy 0.000 description 1
- 238000005286 illumination Methods 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000010166 immunofluorescence Methods 0.000 description 1
- 239000012678 infectious agent Substances 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 239000003999 initiator Substances 0.000 description 1
- 230000004068 intracellular signaling Effects 0.000 description 1
- SZVJSHCCFOBDDC-UHFFFAOYSA-N iron(II,III) oxide Inorganic materials O=[Fe]O[Fe]O[Fe]=O SZVJSHCCFOBDDC-UHFFFAOYSA-N 0.000 description 1
- 229910052747 lanthanoid Inorganic materials 0.000 description 1
- 150000002602 lanthanoids Chemical class 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 108020001756 ligand binding domains Proteins 0.000 description 1
- 231100000149 liver necrosis Toxicity 0.000 description 1
- 238000011866 long-term treatment Methods 0.000 description 1
- 235000020121 low-fat milk Nutrition 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 210000002751 lymph Anatomy 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 239000001115 mace Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 210000003632 microfilament Anatomy 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 230000009149 molecular binding Effects 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 210000002433 mononuclear leukocyte Anatomy 0.000 description 1
- 210000002864 mononuclear phagocyte Anatomy 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 238000011330 nucleic acid test Methods 0.000 description 1
- 210000004940 nucleus Anatomy 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 229940054441 o-phthalaldehyde Drugs 0.000 description 1
- 238000012261 overproduction Methods 0.000 description 1
- 150000003901 oxalic acid esters Chemical class 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 229960003330 pentetic acid Drugs 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- ZWLUXSQADUDCSB-UHFFFAOYSA-N phthalaldehyde Chemical compound O=CC1=CC=CC=C1C=O ZWLUXSQADUDCSB-UHFFFAOYSA-N 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 229920000573 polyethylene Polymers 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 229920001155 polypropylene Polymers 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000025915 regulation of apoptotic process Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 230000036303 septic shock Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 108091006024 signal transducing proteins Proteins 0.000 description 1
- 102000034285 signal transducing proteins Human genes 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000004332 silver Substances 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 230000037351 starvation Effects 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 108020001568 subdomains Proteins 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 208000011580 syndromic disease Diseases 0.000 description 1
- 230000000451 tissue damage Effects 0.000 description 1
- 231100000827 tissue damage Toxicity 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- 238000005829 trimerization reaction Methods 0.000 description 1
- 238000010396 two-hybrid screening Methods 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 230000002792 vascular Effects 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
- 208000016261 weight loss Diseases 0.000 description 1
- 230000004580 weight loss Effects 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
- 238000001086 yeast two-hybrid system Methods 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
- A61K39/3955—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals against proteinaceous materials, e.g. enzymes, hormones, lymphokines
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/40—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against enzymes
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Public Health (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Engineering & Computer Science (AREA)
- Animal Behavior & Ethology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Molecular Biology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Hematology (AREA)
- Diabetes (AREA)
- Endocrinology (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Epidemiology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| IL14527901A IL145279A0 (en) | 2001-09-04 | 2001-09-04 | Antibodies against caspase-8, their preparation and use |
| PCT/IL2002/000734 WO2003020767A2 (en) | 2001-09-04 | 2002-09-04 | Antibodies against caspase-8, their preparation and use |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| UA78526C2 true UA78526C2 (en) | 2007-04-10 |
Family
ID=11075764
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| UA2004042509A UA78526C2 (en) | 2001-09-04 | 2002-04-09 | Antibody against caspase-8, a process for preparation and use of said antibody for development of elisa-analysis |
Country Status (18)
| Country | Link |
|---|---|
| US (2) | US20050058648A1 (el) |
| EP (2) | EP1770101A1 (el) |
| JP (1) | JP2005501905A (el) |
| KR (1) | KR20040044535A (el) |
| CN (1) | CN1599755A (el) |
| AT (1) | ATE335766T1 (el) |
| BR (1) | BR0212289A (el) |
| CA (1) | CA2458985A1 (el) |
| CY (1) | CY1106200T1 (el) |
| DE (1) | DE60213827T2 (el) |
| DK (1) | DK1423429T3 (el) |
| EA (1) | EA009770B1 (el) |
| ES (1) | ES2265511T3 (el) |
| IL (1) | IL145279A0 (el) |
| MX (1) | MXPA04002104A (el) |
| PT (1) | PT1423429E (el) |
| UA (1) | UA78526C2 (el) |
| WO (1) | WO2003020767A2 (el) |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IL158599A0 (en) * | 2003-10-26 | 2004-05-12 | Yeda Res & Dev | Methods of modulating hematopoiesis |
| US7838645B2 (en) * | 2004-04-30 | 2010-11-23 | University Of Maryland College Park | Function of autophagy genes in cell death |
| WO2011049350A2 (ko) * | 2009-10-19 | 2011-04-28 | 한올바이오파마주식회사 | 변형된 인간 종양 괴사 인자 수용체-1 폴리펩티드 또는 그의 절편 및 그의 제조방법 |
| CN106146665B (zh) * | 2016-08-31 | 2019-08-09 | 中国农业科学院植物保护研究所 | 一种用于制备针对甜菜夜蛾caspase-5大亚基的抗体的方法 |
| CN112255061A (zh) * | 2020-10-13 | 2021-01-22 | 南开大学 | 一种通过免疫沉淀分离和检测蛋白质的方法 |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5530101A (en) * | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| WO2000077201A1 (en) * | 1999-06-15 | 2000-12-21 | Astrazeneca Ab | Livin; inhibitor-of-apoptosis protein-3 (iap-3) |
| FR2878852B1 (fr) * | 2000-09-28 | 2007-02-23 | Imtix Sangstat | Procede de production d'immunoglobulines anti-thymocytes humains |
-
2001
- 2001-09-04 IL IL14527901A patent/IL145279A0/xx unknown
-
2002
- 2002-04-09 UA UA2004042509A patent/UA78526C2/uk unknown
- 2002-09-04 US US10/488,608 patent/US20050058648A1/en not_active Abandoned
- 2002-09-04 ES ES02762749T patent/ES2265511T3/es not_active Expired - Lifetime
- 2002-09-04 CA CA002458985A patent/CA2458985A1/en not_active Abandoned
- 2002-09-04 DE DE60213827T patent/DE60213827T2/de not_active Expired - Fee Related
- 2002-09-04 EP EP06014417A patent/EP1770101A1/en not_active Withdrawn
- 2002-09-04 KR KR10-2004-7003217A patent/KR20040044535A/ko not_active Application Discontinuation
- 2002-09-04 JP JP2003525037A patent/JP2005501905A/ja active Pending
- 2002-09-04 MX MXPA04002104A patent/MXPA04002104A/es active IP Right Grant
- 2002-09-04 CN CNA028219678A patent/CN1599755A/zh active Pending
- 2002-09-04 BR BR0212289-8A patent/BR0212289A/pt not_active IP Right Cessation
- 2002-09-04 PT PT02762749T patent/PT1423429E/pt unknown
- 2002-09-04 EA EA200400393A patent/EA009770B1/ru not_active IP Right Cessation
- 2002-09-04 EP EP02762749A patent/EP1423429B1/en not_active Expired - Lifetime
- 2002-09-04 AT AT02762749T patent/ATE335766T1/de not_active IP Right Cessation
- 2002-09-04 WO PCT/IL2002/000734 patent/WO2003020767A2/en active IP Right Grant
- 2002-09-04 DK DK02762749T patent/DK1423429T3/da active
-
2006
- 2006-10-16 CY CY20061101481T patent/CY1106200T1/el unknown
-
2007
- 2007-05-08 US US11/745,949 patent/US20080311599A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| MXPA04002104A (es) | 2004-06-07 |
| US20050058648A1 (en) | 2005-03-17 |
| CN1599755A (zh) | 2005-03-23 |
| EA200400393A1 (ru) | 2004-08-26 |
| EA009770B1 (ru) | 2008-04-28 |
| ES2265511T3 (es) | 2007-02-16 |
| EP1423429B1 (en) | 2006-08-09 |
| IL145279A0 (en) | 2002-06-30 |
| CY1106200T1 (el) | 2011-06-08 |
| JP2005501905A (ja) | 2005-01-20 |
| KR20040044535A (ko) | 2004-05-28 |
| WO2003020767A9 (en) | 2004-04-15 |
| CA2458985A1 (en) | 2003-03-13 |
| EP1770101A1 (en) | 2007-04-04 |
| DK1423429T3 (da) | 2006-09-04 |
| WO2003020767A3 (en) | 2003-10-02 |
| PT1423429E (pt) | 2006-12-29 |
| BR0212289A (pt) | 2004-09-14 |
| DE60213827D1 (de) | 2006-09-21 |
| WO2003020767A2 (en) | 2003-03-13 |
| ATE335766T1 (de) | 2006-09-15 |
| EP1423429A2 (en) | 2004-06-02 |
| DE60213827T2 (de) | 2007-03-29 |
| US20080311599A1 (en) | 2008-12-18 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US8846047B2 (en) | Monoclonal antibodies against HMGB1 | |
| TWI264467B (en) | Human anti-CD40 antibodies and methods of making and using same | |
| JP4382827B2 (ja) | Ａ−３３関連抗原およびそれらの薬理学的使用 | |
| NO327240B1 (no) | Interleukin-18-bindende protein, DNA som koder for dette, vektor og celle inneholdende slikt DNA, fremgangsmate for fremstilling av proteinet, antistoffer som reagerer mot proteinet samt anvendelse av proteinet for fremstilling av medikamenter. | |
| EP2168599B1 (en) | Cancer remedy containing antibody against peptide encoded by exon-17 of periostin | |
| EP0896615B1 (en) | Peptide from soluble form of acetylcholinesterase, active as a calcium channel modulator | |
| US5891437A (en) | Antigen associated with type I diabetes mellitus | |
| KR101154550B1 (ko) | 폰 빌레브란트 인자 특이적 절단 효소에 대한 항체 및그것을 이용한 분석계 | |
| US20080311599A1 (en) | Antibodies against caspase-8, their preparation and use | |
| EA009956B1 (ru) | Внутриклеточный полипептид (cari) и способы его применения | |
| US7544481B1 (en) | Nucleic acids encoding CD40 binding protein | |
| WO2004031241A1 (ja) | ズブチリシン様プロプロテインコンベルターゼ・ｐａｃｅ４に対するモノクローナル抗体及びその利用 | |
| AU2002328090A1 (en) | Antibodies against caspase-8, their preparation and use | |
| JP2004141161A (ja) | ズブチリシン様プロプロテインコンベルターゼ・ｐａｃｅ４に対するモノクローナル抗体及びその利用 | |
| UA76081C2 (en) | Dna sequence coding rip-associated protein (rap-2), competent to replication, expressing vector, transformed host cell, protein rap-2, a method for obtaining thereof, antibody, pharmaceutical composition and methods for modelling of modulated or mediated by protein rip influence on cells | |
| JP2000253881A (ja) | ヒトキャスペース−３（Ｃａｓｐａｓｅ−３）活性誘導物質及びヒトキャスペース−３（Ｃａｓｐａｓｅ−３）活性調節物質 |