JP2001501831A - ガレクチン8、ガレクチン9、ガレクチン10、およびガレクチン10sv - Google Patents
ガレクチン8、ガレクチン9、ガレクチン10、およびガレクチン10svInfo
- Publication number
- JP2001501831A JP2001501831A JP10517750A JP51775098A JP2001501831A JP 2001501831 A JP2001501831 A JP 2001501831A JP 10517750 A JP10517750 A JP 10517750A JP 51775098 A JP51775098 A JP 51775098A JP 2001501831 A JP2001501831 A JP 2001501831A
- Authority
- JP
- Japan
- Prior art keywords
- galectin
- seq
- amino acids
- sequence
- polypeptide
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
Links
- 101001051087 Homo sapiens Galectin-10 Proteins 0.000 title claims abstract description 262
- 102000044466 Galectin-10 Human genes 0.000 title claims abstract description 261
- 102100031351 Galectin-9 Human genes 0.000 title claims abstract description 169
- 101710121810 Galectin-9 Proteins 0.000 title claims abstract description 168
- 101000608769 Homo sapiens Galectin-8 Proteins 0.000 title claims abstract description 156
- 102000044445 Galectin-8 Human genes 0.000 title claims abstract description 152
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 137
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 113
- 229920001184 polypeptide Polymers 0.000 claims abstract description 107
- 102000007563 Galectins Human genes 0.000 claims abstract description 72
- 108010046569 Galectins Proteins 0.000 claims abstract description 72
- 238000000034 method Methods 0.000 claims abstract description 62
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 59
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 50
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 50
- 239000013598 vector Substances 0.000 claims abstract description 45
- 238000010188 recombinant method Methods 0.000 claims abstract description 3
- 239000002773 nucleotide Substances 0.000 claims description 101
- 125000003729 nucleotide group Chemical group 0.000 claims description 97
- 150000001413 amino acids Chemical class 0.000 claims description 73
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 49
- 239000012634 fragment Substances 0.000 claims description 37
- 108091033319 polynucleotide Proteins 0.000 claims description 27
- 102000040430 polynucleotide Human genes 0.000 claims description 27
- 239000002157 polynucleotide Substances 0.000 claims description 26
- 230000000295 complement effect Effects 0.000 claims description 23
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 19
- 239000002253 acid Substances 0.000 claims description 17
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 15
- 238000006467 substitution reaction Methods 0.000 claims description 15
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 14
- 241000124008 Mammalia Species 0.000 claims description 9
- 206010028980 Neoplasm Diseases 0.000 claims description 9
- 201000011510 cancer Diseases 0.000 claims description 8
- 238000009396 hybridization Methods 0.000 claims description 7
- 208000035475 disorder Diseases 0.000 claims description 6
- 238000004519 manufacturing process Methods 0.000 claims description 6
- 208000023275 Autoimmune disease Diseases 0.000 claims description 5
- 208000027866 inflammatory disease Diseases 0.000 claims description 5
- 208000026935 allergic disease Diseases 0.000 claims description 4
- 208000006673 asthma Diseases 0.000 claims description 4
- 238000002955 isolation Methods 0.000 claims description 4
- 230000002062 proliferating effect Effects 0.000 claims description 2
- 230000000717 retained effect Effects 0.000 claims 2
- 206010020751 Hypersensitivity Diseases 0.000 claims 1
- 208000019802 Sexually transmitted disease Diseases 0.000 claims 1
- 230000007815 allergy Effects 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- 108090000623 proteins and genes Proteins 0.000 abstract description 141
- 102000004169 proteins and genes Human genes 0.000 abstract description 102
- 230000000694 effects Effects 0.000 abstract description 29
- 239000005557 antagonist Substances 0.000 abstract description 8
- 239000000556 agonist Substances 0.000 abstract description 6
- 238000012216 screening Methods 0.000 abstract description 6
- 238000002405 diagnostic procedure Methods 0.000 abstract description 4
- 102000050298 human LGALS8 Human genes 0.000 abstract description 4
- 101001130151 Homo sapiens Galectin-9 Proteins 0.000 abstract description 2
- 238000002560 therapeutic procedure Methods 0.000 abstract description 2
- 210000004027 cell Anatomy 0.000 description 98
- 235000018102 proteins Nutrition 0.000 description 92
- 235000001014 amino acid Nutrition 0.000 description 46
- 239000002299 complementary DNA Substances 0.000 description 40
- 108020004414 DNA Proteins 0.000 description 39
- 230000014509 gene expression Effects 0.000 description 36
- 239000013615 primer Substances 0.000 description 35
- 239000013612 plasmid Substances 0.000 description 24
- 108091026890 Coding region Proteins 0.000 description 22
- 241000282414 Homo sapiens Species 0.000 description 22
- 108091008146 restriction endonucleases Proteins 0.000 description 21
- 108020004999 messenger RNA Proteins 0.000 description 18
- 210000001519 tissue Anatomy 0.000 description 14
- 125000000539 amino acid group Chemical group 0.000 description 13
- 210000000349 chromosome Anatomy 0.000 description 13
- 238000010367 cloning Methods 0.000 description 13
- 239000002609 medium Substances 0.000 description 12
- 238000003752 polymerase chain reaction Methods 0.000 description 12
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 11
- 102100021736 Galectin-1 Human genes 0.000 description 11
- 239000013604 expression vector Substances 0.000 description 11
- 238000000746 purification Methods 0.000 description 11
- 241000588724 Escherichia coli Species 0.000 description 10
- 238000004458 analytical method Methods 0.000 description 10
- 108020001507 fusion proteins Proteins 0.000 description 10
- 239000000523 sample Substances 0.000 description 10
- 108010001498 Galectin 1 Proteins 0.000 description 9
- 230000000890 antigenic effect Effects 0.000 description 9
- 230000027455 binding Effects 0.000 description 9
- 150000001875 compounds Chemical class 0.000 description 9
- 201000010099 disease Diseases 0.000 description 9
- 238000005516 engineering process Methods 0.000 description 9
- 102000037865 fusion proteins Human genes 0.000 description 9
- 239000003550 marker Substances 0.000 description 9
- 239000000203 mixture Substances 0.000 description 9
- 230000008488 polyadenylation Effects 0.000 description 9
- 230000014616 translation Effects 0.000 description 9
- 102000053602 DNA Human genes 0.000 description 8
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
- 239000012472 biological sample Substances 0.000 description 8
- 239000002953 phosphate buffered saline Substances 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 238000013519 translation Methods 0.000 description 8
- 239000003155 DNA primer Substances 0.000 description 7
- 239000011543 agarose gel Substances 0.000 description 7
- 229960000723 ampicillin Drugs 0.000 description 7
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 7
- 239000000872 buffer Substances 0.000 description 7
- 230000000875 corresponding effect Effects 0.000 description 7
- 238000013518 transcription Methods 0.000 description 7
- 230000035897 transcription Effects 0.000 description 7
- 238000001890 transfection Methods 0.000 description 7
- 241000894006 Bacteria Species 0.000 description 6
- 241000701022 Cytomegalovirus Species 0.000 description 6
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 6
- 101710198418 Lectin 10 Proteins 0.000 description 6
- 102000004856 Lectins Human genes 0.000 description 6
- 108090001090 Lectins Proteins 0.000 description 6
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 6
- 241000700605 Viruses Species 0.000 description 6
- 230000003321 amplification Effects 0.000 description 6
- 238000003556 assay Methods 0.000 description 6
- 230000036755 cellular response Effects 0.000 description 6
- 238000004587 chromatography analysis Methods 0.000 description 6
- 238000012217 deletion Methods 0.000 description 6
- 230000037430 deletion Effects 0.000 description 6
- 210000003527 eukaryotic cell Anatomy 0.000 description 6
- 230000002068 genetic effect Effects 0.000 description 6
- 230000002163 immunogen Effects 0.000 description 6
- 230000000977 initiatory effect Effects 0.000 description 6
- 210000004962 mammalian cell Anatomy 0.000 description 6
- 229960000485 methotrexate Drugs 0.000 description 6
- 238000003199 nucleic acid amplification method Methods 0.000 description 6
- 241000701447 unidentified baculovirus Species 0.000 description 6
- 102000000802 Galectin 3 Human genes 0.000 description 5
- 108010001517 Galectin 3 Proteins 0.000 description 5
- 241000238631 Hexapoda Species 0.000 description 5
- -1 MGBP Proteins 0.000 description 5
- 108700026244 Open Reading Frames Proteins 0.000 description 5
- ATJFFYVFTNAWJD-UHFFFAOYSA-N Tin Chemical compound [Sn] ATJFFYVFTNAWJD-UHFFFAOYSA-N 0.000 description 5
- 238000011534 incubation Methods 0.000 description 5
- 239000002523 lectin Substances 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 230000004952 protein activity Effects 0.000 description 5
- 238000012163 sequencing technique Methods 0.000 description 5
- 101150051314 tin-10 gene Proteins 0.000 description 5
- 108020004705 Codon Proteins 0.000 description 4
- 101150074155 DHFR gene Proteins 0.000 description 4
- HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 description 4
- 108060003951 Immunoglobulin Proteins 0.000 description 4
- 108091034117 Oligonucleotide Proteins 0.000 description 4
- 101710182846 Polyhedrin Proteins 0.000 description 4
- 108010076504 Protein Sorting Signals Proteins 0.000 description 4
- 230000006907 apoptotic process Effects 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 102000005936 beta-Galactosidase Human genes 0.000 description 4
- 108010005774 beta-Galactosidase Proteins 0.000 description 4
- 238000004113 cell culture Methods 0.000 description 4
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 4
- 230000002759 chromosomal effect Effects 0.000 description 4
- 238000003745 diagnosis Methods 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 230000004927 fusion Effects 0.000 description 4
- 102000018358 immunoglobulin Human genes 0.000 description 4
- 208000015181 infectious disease Diseases 0.000 description 4
- 238000003780 insertion Methods 0.000 description 4
- 230000037431 insertion Effects 0.000 description 4
- 238000013507 mapping Methods 0.000 description 4
- 230000001404 mediated effect Effects 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 239000008194 pharmaceutical composition Substances 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 230000010076 replication Effects 0.000 description 4
- 210000002966 serum Anatomy 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- 241000201370 Autographa californica nucleopolyhedrovirus Species 0.000 description 3
- 241000282693 Cercopithecidae Species 0.000 description 3
- 238000001712 DNA sequencing Methods 0.000 description 3
- 102100024746 Dihydrofolate reductase Human genes 0.000 description 3
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 108091092195 Intron Proteins 0.000 description 3
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 3
- 101710197062 Lectin 8 Proteins 0.000 description 3
- 239000000020 Nitrocellulose Substances 0.000 description 3
- 238000000636 Northern blotting Methods 0.000 description 3
- 238000007792 addition Methods 0.000 description 3
- 239000004202 carbamide Substances 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 238000010276 construction Methods 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 108020001096 dihydrofolate reductase Proteins 0.000 description 3
- 208000023965 endometrium neoplasm Diseases 0.000 description 3
- 229940088598 enzyme Drugs 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 230000012010 growth Effects 0.000 description 3
- 210000003917 human chromosome Anatomy 0.000 description 3
- 238000011065 in-situ storage Methods 0.000 description 3
- 229930027917 kanamycin Natural products 0.000 description 3
- 229960000318 kanamycin Drugs 0.000 description 3
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 3
- 229930182823 kanamycin A Natural products 0.000 description 3
- 239000008101 lactose Substances 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 229920001220 nitrocellulos Polymers 0.000 description 3
- 210000001672 ovary Anatomy 0.000 description 3
- 239000002244 precipitate Substances 0.000 description 3
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 3
- 210000000813 small intestine Anatomy 0.000 description 3
- 239000011734 sodium Substances 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 241001430294 unidentified retrovirus Species 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- NKDFYOWSKOHCCO-YPVLXUMRSA-N 20-hydroxyecdysone Chemical compound C1[C@@H](O)[C@@H](O)C[C@]2(C)[C@@H](CC[C@@]3([C@@H]([C@@](C)(O)[C@H](O)CCC(C)(O)C)CC[C@]33O)C)C3=CC(=O)[C@@H]21 NKDFYOWSKOHCCO-YPVLXUMRSA-N 0.000 description 2
- 229920001817 Agar Polymers 0.000 description 2
- 206010003571 Astrocytoma Diseases 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 101100230428 Caenorhabditis elegans hil-5 gene Proteins 0.000 description 2
- 108091033380 Coding strand Proteins 0.000 description 2
- 108020004635 Complementary DNA Proteins 0.000 description 2
- 102000012410 DNA Ligases Human genes 0.000 description 2
- 108010061982 DNA Ligases Proteins 0.000 description 2
- 229920002307 Dextran Polymers 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 241001131785 Escherichia coli HB101 Species 0.000 description 2
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- 101710154606 Hemagglutinin Proteins 0.000 description 2
- 208000017604 Hodgkin disease Diseases 0.000 description 2
- 208000010747 Hodgkins lymphoma Diseases 0.000 description 2
- 101001042451 Homo sapiens Galectin-1 Proteins 0.000 description 2
- 101000608772 Homo sapiens Galectin-7 Proteins 0.000 description 2
- 229930193140 Neomycin Natural products 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 2
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 2
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 2
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 2
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 2
- 101710176177 Protein A56 Proteins 0.000 description 2
- 108091034057 RNA (poly(A)) Proteins 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 241000714474 Rous sarcoma virus Species 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 230000002776 aggregation Effects 0.000 description 2
- 239000003242 anti bacterial agent Substances 0.000 description 2
- 229940088710 antibiotic agent Drugs 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 238000000376 autoradiography Methods 0.000 description 2
- 210000001124 body fluid Anatomy 0.000 description 2
- 239000010839 body fluid Substances 0.000 description 2
- 239000011575 calcium Substances 0.000 description 2
- 239000001506 calcium phosphate Substances 0.000 description 2
- 229910000389 calcium phosphate Inorganic materials 0.000 description 2
- 235000011010 calcium phosphates Nutrition 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 230000010261 cell growth Effects 0.000 description 2
- 239000013592 cell lysate Substances 0.000 description 2
- 230000008619 cell matrix interaction Effects 0.000 description 2
- 230000004663 cell proliferation Effects 0.000 description 2
- 238000012761 co-transfection Methods 0.000 description 2
- 210000001072 colon Anatomy 0.000 description 2
- 229960002086 dextran Drugs 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 210000000981 epithelium Anatomy 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- 210000002458 fetal heart Anatomy 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- 230000005021 gait Effects 0.000 description 2
- 108010065785 galectin 5 Proteins 0.000 description 2
- 210000002216 heart Anatomy 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 239000000710 homodimer Substances 0.000 description 2
- 102000058212 human LGALS7 Human genes 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 238000007901 in situ hybridization Methods 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 210000003000 inclusion body Anatomy 0.000 description 2
- 238000001802 infusion Methods 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 230000000968 intestinal effect Effects 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 238000002372 labelling Methods 0.000 description 2
- 201000007270 liver cancer Diseases 0.000 description 2
- 208000014018 liver neoplasm Diseases 0.000 description 2
- 210000004072 lung Anatomy 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 201000001441 melanoma Diseases 0.000 description 2
- 230000031864 metaphase Effects 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 229960004927 neomycin Drugs 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 210000004940 nucleus Anatomy 0.000 description 2
- 210000000496 pancreas Anatomy 0.000 description 2
- 201000002528 pancreatic cancer Diseases 0.000 description 2
- 238000010647 peptide synthesis reaction Methods 0.000 description 2
- 210000002381 plasma Anatomy 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 239000002987 primer (paints) Substances 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 238000003127 radioimmunoassay Methods 0.000 description 2
- 238000010839 reverse transcription Methods 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 102220240796 rs553605556 Human genes 0.000 description 2
- 230000003248 secreting effect Effects 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 239000006152 selective media Substances 0.000 description 2
- 210000002027 skeletal muscle Anatomy 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 210000000952 spleen Anatomy 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 2
- 210000002700 urine Anatomy 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 210000005253 yeast cell Anatomy 0.000 description 2
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 1
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 1
- 241001514645 Agonis Species 0.000 description 1
- 206010003210 Arteriosclerosis Diseases 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- 206010005949 Bone cancer Diseases 0.000 description 1
- 208000018084 Bone neoplasm Diseases 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 206010006187 Breast cancer Diseases 0.000 description 1
- 208000026310 Breast neoplasm Diseases 0.000 description 1
- 108091028026 C-DNA Proteins 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 229920000832 Cutin Polymers 0.000 description 1
- 230000004544 DNA amplification Effects 0.000 description 1
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
- 241000257465 Echinoidea Species 0.000 description 1
- 206010014733 Endometrial cancer Diseases 0.000 description 1
- 206010014759 Endometrial neoplasm Diseases 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 241001596967 Escherichia coli M15 Species 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 101710121821 Galectin-6 Proteins 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 108010093488 His-His-His-His-His-His Proteins 0.000 description 1
- 101000756632 Homo sapiens Actin, cytoplasmic 1 Proteins 0.000 description 1
- 101001042446 Homo sapiens Galectin-2 Proteins 0.000 description 1
- 101000608757 Homo sapiens Galectin-3 Proteins 0.000 description 1
- 102000002265 Human Growth Hormone Human genes 0.000 description 1
- 108010000521 Human Growth Hormone Proteins 0.000 description 1
- 239000000854 Human Growth Hormone Substances 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 241000701024 Human betaherpesvirus 5 Species 0.000 description 1
- 208000008839 Kidney Neoplasms Diseases 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- 108010054278 Lac Repressors Proteins 0.000 description 1
- 101710197064 Lectin 9 Proteins 0.000 description 1
- 206010058467 Lung neoplasm malignant Diseases 0.000 description 1
- 101710141347 Major envelope glycoprotein Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 101100278853 Mus musculus Dhfr gene Proteins 0.000 description 1
- 102100025243 Myeloid cell surface antigen CD33 Human genes 0.000 description 1
- 238000005481 NMR spectroscopy Methods 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 206010033128 Ovarian cancer Diseases 0.000 description 1
- 206010061535 Ovarian neoplasm Diseases 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 241000286209 Phasianidae Species 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 206010036790 Productive cough Diseases 0.000 description 1
- 206010060862 Prostate cancer Diseases 0.000 description 1
- 208000000236 Prostatic Neoplasms Diseases 0.000 description 1
- 239000012083 RIPA buffer Substances 0.000 description 1
- 101000608761 Rattus norvegicus Galectin-3 Proteins 0.000 description 1
- 101000608762 Rattus norvegicus Galectin-4 Proteins 0.000 description 1
- 206010038389 Renal cancer Diseases 0.000 description 1
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 description 1
- 108091081021 Sense strand Proteins 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 1
- 241000409492 Simian enterovirus SV4 Species 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 244000061458 Solanum melongena Species 0.000 description 1
- 235000002597 Solanum melongena Nutrition 0.000 description 1
- 208000000277 Splenic Neoplasms Diseases 0.000 description 1
- 241000256248 Spodoptera Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
- 230000033540 T cell apoptotic process Effects 0.000 description 1
- 208000000389 T-cell leukemia Diseases 0.000 description 1
- 208000028530 T-cell lymphoblastic leukemia/lymphoma Diseases 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- GKLVYJBZJHMRIY-OUBTZVSYSA-N Technetium-99 Chemical compound [99Tc] GKLVYJBZJHMRIY-OUBTZVSYSA-N 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 101100002024 Thermus aquaticus pstI gene Proteins 0.000 description 1
- 108091036066 Three prime untranslated region Proteins 0.000 description 1
- 108010022394 Threonine synthase Proteins 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- YZCKVEUIGOORGS-NJFSPNSNSA-N Tritium Chemical compound [3H] YZCKVEUIGOORGS-NJFSPNSNSA-N 0.000 description 1
- 108020005202 Viral DNA Proteins 0.000 description 1
- HMNZFMSWFCAGGW-XPWSMXQVSA-N [3-[hydroxy(2-hydroxyethoxy)phosphoryl]oxy-2-[(e)-octadec-9-enoyl]oxypropyl] (e)-octadec-9-enoate Chemical compound CCCCCCCC\C=C\CCCCCCCC(=O)OCC(COP(O)(=O)OCCO)OC(=O)CCCCCCC\C=C\CCCCCCCC HMNZFMSWFCAGGW-XPWSMXQVSA-N 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000005054 agglomeration Methods 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 238000012867 alanine scanning Methods 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
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 238000005349 anion exchange Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 230000009830 antibody antigen interaction Effects 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 208000011775 arteriosclerosis disease Diseases 0.000 description 1
- 108010044715 asialofetuin Proteins 0.000 description 1
- 230000003416 augmentation Effects 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 210000001185 bone marrow Anatomy 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 150000001720 carbohydrates Chemical group 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 238000005341 cation exchange Methods 0.000 description 1
- 230000021164 cell adhesion Effects 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 230000030833 cell death Effects 0.000 description 1
- 230000035289 cell-matrix adhesion Effects 0.000 description 1
- 210000003570 cell-matrix junction Anatomy 0.000 description 1
- 108091092328 cellular RNA Proteins 0.000 description 1
- 210000001175 cerebrospinal fluid Anatomy 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 230000000973 chemotherapeutic effect Effects 0.000 description 1
- 238000003200 chromosome mapping Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 238000002425 crystallisation Methods 0.000 description 1
- 230000008025 crystallization Effects 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000030609 dephosphorylation Effects 0.000 description 1
- 238000006209 dephosphorylation reaction Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 229960000633 dextran sulfate Drugs 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 102000004419 dihydrofolate reductase Human genes 0.000 description 1
- OZRNSSUDZOLUSN-LBPRGKRZSA-N dihydrofolic acid Chemical compound N=1C=2C(=O)NC(N)=NC=2NCC=1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 OZRNSSUDZOLUSN-LBPRGKRZSA-N 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 239000006196 drop Substances 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 230000008482 dysregulation Effects 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 230000002357 endometrial effect Effects 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- ZINJLDJMHCUBIP-UHFFFAOYSA-N ethametsulfuron-methyl Chemical compound CCOC1=NC(NC)=NC(NC(=O)NS(=O)(=O)C=2C(=CC=CC=2)C(=O)OC)=N1 ZINJLDJMHCUBIP-UHFFFAOYSA-N 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 230000029142 excretion Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000003889 eye drop Substances 0.000 description 1
- 229940012356 eye drops Drugs 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 235000019688 fish Nutrition 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 230000037433 frameshift Effects 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 108060003196 globin Proteins 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 239000006451 grace's insect medium Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 235000012907 honey Nutrition 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 102000045521 human LGALS1 Human genes 0.000 description 1
- 102000048551 human LGALS3 Human genes 0.000 description 1
- 102000056349 human LGALS9 Human genes 0.000 description 1
- 102000006446 human galectin 10 Human genes 0.000 description 1
- 210000004754 hybrid cell Anatomy 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
- 230000036737 immune function Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 229910052738 indium Inorganic materials 0.000 description 1
- APFVFJFRJDLVQX-UHFFFAOYSA-N indium atom Chemical compound [In] APFVFJFRJDLVQX-UHFFFAOYSA-N 0.000 description 1
- 206010022000 influenza Diseases 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000008611 intercellular interaction Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 229910052740 iodine Inorganic materials 0.000 description 1
- 239000011630 iodine Substances 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 201000010982 kidney cancer Diseases 0.000 description 1
- 101150109249 lacI gene Proteins 0.000 description 1
- 101150085091 lat-2 gene Proteins 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 238000007834 ligase chain reaction Methods 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000009630 liquid culture Methods 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 201000005202 lung cancer Diseases 0.000 description 1
- 208000020816 lung neoplasm Diseases 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 208000015486 malignant pancreatic neoplasm Diseases 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 239000002808 molecular sieve Substances 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 150000003833 nucleoside derivatives Chemical class 0.000 description 1
- 239000002674 ointment Substances 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 208000008443 pancreatic carcinoma Diseases 0.000 description 1
- 244000045947 parasite Species 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 1
- 229910000498 pewter Inorganic materials 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 229940080469 phosphocellulose Drugs 0.000 description 1
- 238000005222 photoaffinity labeling Methods 0.000 description 1
- 239000000049 pigment Substances 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 108010066381 preproinsulin Proteins 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 238000004393 prognosis Methods 0.000 description 1
- 210000002307 prostate Anatomy 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 230000012846 protein folding Effects 0.000 description 1
- 230000004853 protein function Effects 0.000 description 1
- 108020001775 protein parts Proteins 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- 230000001105 regulatory effect Effects 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
- 210000003705 ribosome Anatomy 0.000 description 1
- 108010038196 saccharide-binding proteins Proteins 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 230000001568 sexual effect Effects 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000004332 silver Substances 0.000 description 1
- 230000002226 simultaneous effect Effects 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 230000035943 smell Effects 0.000 description 1
- 210000002460 smooth muscle Anatomy 0.000 description 1
- URGAHOPLAPQHLN-UHFFFAOYSA-N sodium aluminosilicate Chemical compound [Na+].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O URGAHOPLAPQHLN-UHFFFAOYSA-N 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 201000002471 spleen cancer Diseases 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 210000003802 sputum Anatomy 0.000 description 1
- 208000024794 sputum Diseases 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- 125000001424 substituent group Chemical group 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 210000001179 synovial fluid Anatomy 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 210000001550 testis Anatomy 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 229940126585 therapeutic drug Drugs 0.000 description 1
- ANRHNWWPFJCPAZ-UHFFFAOYSA-M thionine Chemical compound [Cl-].C1=CC(N)=CC2=[S+]C3=CC(N)=CC=C3N=C21 ANRHNWWPFJCPAZ-UHFFFAOYSA-M 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 230000005026 transcription initiation Effects 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 230000010474 transient expression Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- HRXKRNGNAMMEHJ-UHFFFAOYSA-K trisodium citrate Chemical compound [Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O HRXKRNGNAMMEHJ-UHFFFAOYSA-K 0.000 description 1
- 229940038773 trisodium citrate Drugs 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 229910052722 tritium Inorganic materials 0.000 description 1
- 210000003954 umbilical cord Anatomy 0.000 description 1
- 230000009452 underexpressoin Effects 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 230000007442 viral DNA synthesis Effects 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
- A61P11/06—Antiasthmatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/10—Antimycotics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P33/00—Antiparasitic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- 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
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- 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
- A61P37/08—Antiallergic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4726—Lectins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
- G01N2333/46—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans from vertebrates
- G01N2333/47—Assays involving proteins of known structure or function as defined in the subgroups
- G01N2333/4701—Details
- G01N2333/4724—Lectins
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Veterinary Medicine (AREA)
- General Chemical & Material Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Animal Behavior & Ethology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Public Health (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Immunology (AREA)
- Pulmonology (AREA)
- Oncology (AREA)
- Urology & Nephrology (AREA)
- Communicable Diseases (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- Heart & Thoracic Surgery (AREA)
- Hematology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Cardiology (AREA)
- Dermatology (AREA)
- Biotechnology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Rheumatology (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Pain & Pain Management (AREA)
- Transplantation (AREA)
- Tropical Medicine & Parasitology (AREA)
- Virology (AREA)
- Toxicology (AREA)
- Cell Biology (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US2809396P | 1996-10-09 | 1996-10-09 | |
| WO96/16565 | 1996-10-09 | ||
| US9616565 | 1996-10-09 | ||
| WO60/028,093 | 1996-10-09 | ||
| PCT/US1997/018261 WO1998015624A1 (fr) | 1996-10-09 | 1997-10-09 | Galectine 8, 9, 10, et 10sv |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2001501831A true JP2001501831A (ja) | 2001-02-13 |
| JP2001501831A5 JP2001501831A5 (fr) | 2005-06-16 |
Family
ID=26703285
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP10517750A Withdrawn JP2001501831A (ja) | 1996-10-09 | 1997-10-09 | ガレクチン8、ガレクチン9、ガレクチン10、およびガレクチン10sv |
Country Status (4)
| Country | Link |
|---|---|
| EP (1) | EP1012266A4 (fr) |
| JP (1) | JP2001501831A (fr) |
| CA (1) | CA2268022A1 (fr) |
| WO (1) | WO1998015624A1 (fr) |
Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2005121340A1 (fr) * | 2004-06-14 | 2005-12-22 | Galpharma Co., Ltd. | Nouvelle protéine de modification galectine 8 et utilisation de celle-ci |
| JP2007131540A (ja) * | 2005-11-08 | 2007-05-31 | Galpharma Co Ltd | Cd44機能抑制因子による抗アレルギー薬、免疫抑制薬および抗腫瘍薬 |
| JP2008500013A (ja) * | 2003-10-03 | 2008-01-10 | ザ ブライハム アンド ウイメンズ ホスピタル,インコーポレイテッド | Tim−3ポリペプチド |
| JPWO2005093064A1 (ja) * | 2004-03-29 | 2008-02-14 | 株式会社ガルファーマ | 新規ガレクチン9改変体タンパク質及びその用途 |
| JP5420791B1 (ja) * | 2013-08-23 | 2014-02-19 | 肇 福永 | サルモネラ菌及びシート状m細胞 |
| WO2014171018A1 (fr) * | 2013-04-20 | 2014-10-23 | 株式会社ガルファーマ | Procédé permettant de diagnostiquer une maladie (ou des maladies), procédé permettant de traiter ou de prévenir une maladie (ou des maladies), kit permettant de diagnostiquer une maladie (ou des maladies), et médicament permettant de traiter ou de prévenir une maladie (ou des maladies) |
| JP2019131531A (ja) * | 2018-01-29 | 2019-08-08 | 日本メナード化粧品株式会社 | ガレクチン−9産生促進剤 |
Families Citing this family (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IL139945A0 (en) * | 1998-06-03 | 2002-02-10 | Effector Cell Inst | Eosinophil chemotactic factor |
| CN1302881A (zh) | 1999-10-28 | 2001-07-11 | 上海博容基因开发有限公司 | 一种新的多肽——人β-半乳糖苷结合蛋白和编码这种多肽的多核苷酸 |
| US6953658B2 (en) | 2000-03-09 | 2005-10-11 | Diadexus, Inc. | Method of diagnosing, monitoring, staging, imaging and treating gastrointestinal cancer |
| EP1331483A4 (fr) * | 2000-11-01 | 2007-06-20 | Galpharma Co Ltd | Agent permettant de detecter l'aptitude d'une tumeur cancereuse a se metastaser |
| EP1490403A2 (fr) * | 2002-02-28 | 2004-12-29 | YEDA RESEARCH AND DEVELOPMENT Co. LTD. | Agents de liaison de glycoproteines cd44 et methodes d'utilisation associees |
| WO2003074673A2 (fr) * | 2002-03-01 | 2003-09-12 | Exelixis, Inc. | Lgals tenant lieu de modificateurs de la voie de chk et leurs procedes d'utilisation |
| EP1569675A4 (fr) * | 2002-11-14 | 2009-08-12 | Yissum Res Dev Co | Nouvelles sequences de galectine, et compositions et methodes utilisant celles-ci pour traiter ou diagnostiquer l'arthrite et d'autres maladies inflammatoires chroniques |
| US20060009378A1 (en) | 2002-11-14 | 2006-01-12 | Itshak Golan | Novel galectin sequences and compositions and methods utilizing same for treating or diagnosing arthritis and other chronic inflammatory diseases |
| EP1586325A1 (fr) * | 2003-01-24 | 2005-10-19 | Galpharma Co., Ltd. | Medicaments contenant galectine 9 |
| WO2004096851A1 (fr) * | 2003-04-28 | 2004-11-11 | Galpharma Co., Ltd. | Facteur d'induction de la galectine 9 |
| DE10333406A1 (de) * | 2003-07-15 | 2005-02-10 | Protagen Ag | T-regulatorische-Zellen enthaltend Galectine zur Therapie und Diagnose von Erkrankungen |
| TW200539890A (en) | 2004-03-12 | 2005-12-16 | Brigham & Womens Hospital | Methods of modulating immune responses by modulating tim-1, tim-2 and tim-4 function |
| CN1332030C (zh) * | 2005-04-28 | 2007-08-15 | 武汉大学 | 一种真菌半乳糖凝集素蛋白活性的多肽、其编码序列及制备方法和应用 |
| CN102205111B (zh) * | 2011-05-19 | 2013-01-23 | 武汉大学 | 杨树菇半乳糖凝集素在制备抗hiv感染药物中的用途 |
| AU2017264754A1 (en) * | 2016-05-10 | 2018-12-13 | Genentech, Inc. | Methods of decreasing trisulfide bonds during recombinant production of polypeptides |
| CN108409850A (zh) * | 2018-01-30 | 2018-08-17 | 河南师范大学 | 一种鱼源半乳糖凝集素CaGal重组蛋白的制备方法及其应用 |
| CN113999287B (zh) * | 2021-12-02 | 2023-06-27 | 深圳湾实验室坪山生物医药研发转化中心 | 一种靶向半乳糖凝集素-10的多肽抑制剂及其制备方法和用途 |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5851764A (en) * | 1990-10-25 | 1998-12-22 | The Trustees Of Columbia University In The City Of New York | Human prostate tumor inducing gene-1 and uses thereof |
| CA2221798A1 (fr) * | 1995-06-06 | 1996-12-12 | Human Genome Sciences, Inc. | Genes et proteines specifiques du colon |
| WO1997003190A1 (fr) * | 1995-07-11 | 1997-01-30 | Sagami Chemical Research Center | PROTEINE HUMAINE SEMBLABLE A GALECTINE-4 ET ADNc CODANT CETTE PROTEINE |
-
1997
- 1997-10-09 WO PCT/US1997/018261 patent/WO1998015624A1/fr not_active Application Discontinuation
- 1997-10-09 CA CA002268022A patent/CA2268022A1/fr not_active Abandoned
- 1997-10-09 JP JP10517750A patent/JP2001501831A/ja not_active Withdrawn
- 1997-10-09 EP EP97912689A patent/EP1012266A4/fr not_active Withdrawn
Cited By (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2012006959A (ja) * | 2003-10-03 | 2012-01-12 | Brigham & Womens Hospital Inc | Tim−3ポリペプチド |
| JP2014039558A (ja) * | 2003-10-03 | 2014-03-06 | Brigham & Women's Hospital Inc | Tim−3ポリペプチド |
| JP2008500013A (ja) * | 2003-10-03 | 2008-01-10 | ザ ブライハム アンド ウイメンズ ホスピタル,インコーポレイテッド | Tim−3ポリペプチド |
| JPWO2005093064A1 (ja) * | 2004-03-29 | 2008-02-14 | 株式会社ガルファーマ | 新規ガレクチン9改変体タンパク質及びその用途 |
| JP4792390B2 (ja) * | 2004-03-29 | 2011-10-12 | 株式会社ガルファーマ | 新規ガレクチン9改変体タンパク質及びその用途 |
| US8268324B2 (en) | 2004-03-29 | 2012-09-18 | Galpharma Co., Ltd. | Modified galectin 9 proteins and use thereof |
| US8580743B2 (en) | 2004-03-29 | 2013-11-12 | Galpharma Co., Ltd. | Modified galectin 9 proteins and methods of treatment using them |
| JPWO2005121340A1 (ja) * | 2004-06-14 | 2008-04-10 | 株式会社ガルファーマ | 新規ガレクチン8改変体タンパク質及びその用途 |
| WO2005121340A1 (fr) * | 2004-06-14 | 2005-12-22 | Galpharma Co., Ltd. | Nouvelle protéine de modification galectine 8 et utilisation de celle-ci |
| JP2007131540A (ja) * | 2005-11-08 | 2007-05-31 | Galpharma Co Ltd | Cd44機能抑制因子による抗アレルギー薬、免疫抑制薬および抗腫瘍薬 |
| WO2014171018A1 (fr) * | 2013-04-20 | 2014-10-23 | 株式会社ガルファーマ | Procédé permettant de diagnostiquer une maladie (ou des maladies), procédé permettant de traiter ou de prévenir une maladie (ou des maladies), kit permettant de diagnostiquer une maladie (ou des maladies), et médicament permettant de traiter ou de prévenir une maladie (ou des maladies) |
| JP5420791B1 (ja) * | 2013-08-23 | 2014-02-19 | 肇 福永 | サルモネラ菌及びシート状m細胞 |
| WO2015025638A1 (fr) * | 2013-08-23 | 2015-02-26 | ケイ・アンド・アイ有限会社 | Salmonella et cellules m de type feuille |
| JP2019131531A (ja) * | 2018-01-29 | 2019-08-08 | 日本メナード化粧品株式会社 | ガレクチン−9産生促進剤 |
| JP7224583B2 (ja) | 2018-01-29 | 2023-02-20 | 日本メナード化粧品株式会社 | ガレクチン-9産生促進剤 |
Also Published As
| Publication number | Publication date |
|---|---|
| CA2268022A1 (fr) | 1998-04-16 |
| WO1998015624A1 (fr) | 1998-04-16 |
| EP1012266A4 (fr) | 2004-04-28 |
| EP1012266A1 (fr) | 2000-06-28 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| KR100497017B1 (ko) | 고사유도분자ii | |
| JP2001501831A (ja) | ガレクチン8、ガレクチン9、ガレクチン10、およびガレクチン10sv | |
| JP2002508657A (ja) | 2つのヒトgタンパク質共役型レセプター:ebv誘導性gpcr2(ebi−2)およびedg−1様gpcr | |
| KR20010012554A (ko) | 항미생물성 펩티드 | |
| WO1998015624A9 (fr) | Galectine 8, 9, 10, et 10sv | |
| JPH10509328A (ja) | ケラチノサイト増殖因子−2 | |
| US6468768B1 (en) | Galectin 9 and 10SV polynucleotides | |
| US5710024A (en) | Polynucleotides that encode the calcitonin gene-related peptide receptor coponent factor (HOUNDC44) | |
| US6329169B1 (en) | Nucleic acid molecules encoding cytostatin II | |
| EP0879887A1 (fr) | Un gène humain ressemblant à la protéine murine secretée SDF5 (ATG-1622) | |
| JP2001507227A (ja) | 小脳および胚に特異的なタンパク質 | |
| JPH11506341A (ja) | Gタンパク質レセプターhtnad29 | |
| EP0884386A1 (fr) | Canaux récepteurs de sodium | |
| JP2001504336A (ja) | 結合組織増殖因子―3 | |
| KR19990007806A (ko) | 전환 성장 인자 α HII | |
| JP2003512291A (ja) | ガレクチン11 | |
| US20070020277A1 (en) | Human Oncogene Induced Secreted Protein I | |
| JP2000106889A (ja) | 分泌マウスタンパク質sFRP―1に類似した新規ヒト遺伝子 | |
| JPH114698A (ja) | 分泌性タンパク質Frizbと類似する新規ヒト遺伝子(ATG−1639) | |
| JP3759168B2 (ja) | 内皮単球活性ポリペプチドiii | |
| US20020173000A1 (en) | Sodium channel receptor | |
| JPH1175865A (ja) | 分泌ネズミ・蛋白sdf5に類似したヒト・遺伝子(atg−1622) | |
| KR19990008320A (ko) | 사람 뉴로펩티드 수용체 | |
| AU2004202460A1 (en) | Apoptosis Inducing Molecule II | |
| CA2402839A1 (fr) | Galectine 11 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20041008 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20041008 |
|
| A761 | Written withdrawal of application |
Free format text: JAPANESE INTERMEDIATE CODE: A761 Effective date: 20060303 |