IL88322A - Monoclonal antibodies capable of recognizing n-acetylneuraminic acid in beta-arrangement used for diagnosis and prognosis of tumors and acute inflammatory diseases - Google Patents
Monoclonal antibodies capable of recognizing n-acetylneuraminic acid in beta-arrangement used for diagnosis and prognosis of tumors and acute inflammatory diseasesInfo
- Publication number
- IL88322A IL88322A IL8832288A IL8832288A IL88322A IL 88322 A IL88322 A IL 88322A IL 8832288 A IL8832288 A IL 8832288A IL 8832288 A IL8832288 A IL 8832288A IL 88322 A IL88322 A IL 88322A
- Authority
- IL
- Israel
- Prior art keywords
- set forth
- acetylneuraminic acid
- cells
- beta
- monoclonal antibody
- Prior art date
Links
- SQVRNKJHWKZAKO-PFQGKNLYSA-N N-acetyl-beta-neuraminic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-PFQGKNLYSA-N 0.000 title claims description 49
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 title claims description 40
- 230000001154 acute effect Effects 0.000 title claims description 6
- 238000003745 diagnosis Methods 0.000 title claims description 6
- 208000027866 inflammatory disease Diseases 0.000 title claims description 6
- 206010028980 Neoplasm Diseases 0.000 title description 4
- 238000004393 prognosis Methods 0.000 title description 3
- 210000004408 hybridoma Anatomy 0.000 claims description 37
- 238000000034 method Methods 0.000 claims description 36
- 210000004027 cell Anatomy 0.000 claims description 22
- 239000000427 antigen Substances 0.000 claims description 20
- 102000036639 antigens Human genes 0.000 claims description 20
- 108091007433 antigens Proteins 0.000 claims description 20
- 150000001875 compounds Chemical class 0.000 claims description 20
- 206010035226 Plasma cell myeloma Diseases 0.000 claims description 14
- 201000000050 myeloid neoplasm Diseases 0.000 claims description 14
- 241001465754 Metazoa Species 0.000 claims description 12
- 230000000890 antigenic effect Effects 0.000 claims description 10
- 210000003719 b-lymphocyte Anatomy 0.000 claims description 9
- 230000007910 cell fusion Effects 0.000 claims description 9
- 230000003053 immunization Effects 0.000 claims description 9
- 238000002649 immunization Methods 0.000 claims description 6
- 210000004989 spleen cell Anatomy 0.000 claims description 6
- 241000607142 Salmonella Species 0.000 claims description 5
- 239000002671 adjuvant Substances 0.000 claims description 5
- 210000004698 lymphocyte Anatomy 0.000 claims description 5
- 239000002202 Polyethylene glycol Substances 0.000 claims description 4
- 210000004369 blood Anatomy 0.000 claims description 4
- 239000008280 blood Substances 0.000 claims description 4
- 201000011510 cancer Diseases 0.000 claims description 4
- 239000003795 chemical substances by application Substances 0.000 claims description 4
- 229920001223 polyethylene glycol Polymers 0.000 claims description 4
- 210000002700 urine Anatomy 0.000 claims description 4
- 238000004519 manufacturing process Methods 0.000 claims description 3
- 230000016784 immunoglobulin production Effects 0.000 claims description 2
- 108060003951 Immunoglobulin Proteins 0.000 claims 1
- 102000018358 immunoglobulin Human genes 0.000 claims 1
- 239000000243 solution Substances 0.000 description 23
- 238000009739 binding Methods 0.000 description 9
- 239000002609 medium Substances 0.000 description 9
- 239000002953 phosphate buffered saline Substances 0.000 description 9
- 239000001963 growth medium Substances 0.000 description 8
- 230000002163 immunogen Effects 0.000 description 7
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 230000037029 cross reaction Effects 0.000 description 5
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 4
- 241000699670 Mus sp. Species 0.000 description 4
- 239000012980 RPMI-1640 medium Substances 0.000 description 4
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 230000002860 competitive effect Effects 0.000 description 4
- 239000012091 fetal bovine serum Substances 0.000 description 4
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 235000014633 carbohydrates Nutrition 0.000 description 3
- 150000001720 carbohydrates Chemical class 0.000 description 3
- 239000005018 casein Substances 0.000 description 3
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 3
- 235000021240 caseins Nutrition 0.000 description 3
- 230000002401 inhibitory effect Effects 0.000 description 3
- 239000011550 stock solution Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- MSWZFWKMSRAUBD-IVMDWMLBSA-N 2-amino-2-deoxy-D-glucopyranose Chemical compound N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O MSWZFWKMSRAUBD-IVMDWMLBSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 2
- 241000699666 Mus <mouse, genus> Species 0.000 description 2
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 2
- 241000276498 Pollachius virens Species 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- MSWZFWKMSRAUBD-UHFFFAOYSA-N beta-D-galactosamine Natural products NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 0.000 description 2
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- 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 2
- 239000012153 distilled water Substances 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 229960002442 glucosamine Drugs 0.000 description 2
- 238000011835 investigation Methods 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- DAEPDZWVDSPTHF-UHFFFAOYSA-M sodium pyruvate Chemical compound [Na+].CC(=O)C([O-])=O DAEPDZWVDSPTHF-UHFFFAOYSA-M 0.000 description 2
- 210000000952 spleen Anatomy 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 229940104230 thymidine Drugs 0.000 description 2
- WYWHKKSPHMUBEB-UHFFFAOYSA-N tioguanine Chemical compound N1C(N)=NC(=S)C2=C1N=CN2 WYWHKKSPHMUBEB-UHFFFAOYSA-N 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- GEYOCULIXLDCMW-UHFFFAOYSA-N 1,2-phenylenediamine Chemical compound NC1=CC=CC=C1N GEYOCULIXLDCMW-UHFFFAOYSA-N 0.000 description 1
- WEEMDRWIKYCTQM-UHFFFAOYSA-N 2,6-dimethoxybenzenecarbothioamide Chemical compound COC1=CC=CC(OC)=C1C(N)=S WEEMDRWIKYCTQM-UHFFFAOYSA-N 0.000 description 1
- GHCZTIFQWKKGSB-UHFFFAOYSA-N 2-hydroxypropane-1,2,3-tricarboxylic acid;phosphoric acid Chemical compound OP(O)(O)=O.OC(=O)CC(O)(C(O)=O)CC(O)=O GHCZTIFQWKKGSB-UHFFFAOYSA-N 0.000 description 1
- HVCOBJNICQPDBP-UHFFFAOYSA-N 3-[3-[3,5-dihydroxy-6-methyl-4-(3,4,5-trihydroxy-6-methyloxan-2-yl)oxyoxan-2-yl]oxydecanoyloxy]decanoic acid;hydrate Chemical compound O.OC1C(OC(CC(=O)OC(CCCCCCC)CC(O)=O)CCCCCCC)OC(C)C(O)C1OC1C(O)C(O)C(O)C(C)O1 HVCOBJNICQPDBP-UHFFFAOYSA-N 0.000 description 1
- TVZGACDUOSZQKY-LBPRGKRZSA-N 4-aminofolic acid Chemical compound C1=NC2=NC(N)=NC(N)=C2N=C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 TVZGACDUOSZQKY-LBPRGKRZSA-N 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 229930186217 Glycolipid Natural products 0.000 description 1
- 208000032843 Hemorrhage Diseases 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 102000005348 Neuraminidase Human genes 0.000 description 1
- 108010006232 Neuraminidase Proteins 0.000 description 1
- 239000004105 Penicillin G potassium Substances 0.000 description 1
- 229920001030 Polyethylene Glycol 4000 Polymers 0.000 description 1
- 102000003838 Sialyltransferases Human genes 0.000 description 1
- 108090000141 Sialyltransferases Proteins 0.000 description 1
- 125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 229960003896 aminopterin Drugs 0.000 description 1
- 210000000628 antibody-producing cell Anatomy 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 230000000740 bleeding effect Effects 0.000 description 1
- 238000009395 breeding Methods 0.000 description 1
- 230000001488 breeding effect Effects 0.000 description 1
- 229920001429 chelating resin Polymers 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000004737 colorimetric analysis Methods 0.000 description 1
- 230000001143 conditioned effect Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000003113 dilution method Methods 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 238000013399 early diagnosis Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 229920000609 methyl cellulose Polymers 0.000 description 1
- 239000001923 methylcellulose Substances 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 235000019368 penicillin G potassium Nutrition 0.000 description 1
- 229940056360 penicillin g Drugs 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 235000018102 proteins Nutrition 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical class CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 description 1
- 229940054269 sodium pyruvate Drugs 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 229960002385 streptomycin sulfate Drugs 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 229960003087 tioguanine Drugs 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- 239000000439 tumor marker Substances 0.000 description 1
- 238000005406 washing 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/10—Cells modified by introduction of foreign genetic material
- C12N5/12—Fused cells, e.g. hybridomas
- C12N5/16—Animal cells
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Immunology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Wood Science & Technology (AREA)
- Biophysics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Zoology (AREA)
- Microbiology (AREA)
- Cell Biology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Pharmacology & Pharmacy (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Epidemiology (AREA)
- Mycology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP28711987 | 1987-11-13 | ||
| JP63026848A JPH02486A (ja) | 1987-11-13 | 1988-02-08 | 遊離ｎ−アセチルノイラミン酸を認識するモノクローナル抗体 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| IL88322A true IL88322A (en) | 1994-05-30 |
Family
ID=26364692
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IL8832288A IL88322A (en) | 1987-11-13 | 1988-11-08 | Monoclonal antibodies capable of recognizing n-acetylneuraminic acid in beta-arrangement used for diagnosis and prognosis of tumors and acute inflammatory diseases |
Country Status (13)
| Country | Link |
|---|---|
| US (1) | US5158886A (ja) |
| EP (1) | EP0316818B1 (ja) |
| JP (1) | JPH02486A (ja) |
| KR (1) | KR960004855B1 (ja) |
| AU (1) | AU614553B2 (ja) |
| CA (1) | CA1336763C (ja) |
| DE (1) | DE3881344T2 (ja) |
| ES (1) | ES2054772T3 (ja) |
| FI (1) | FI90989C (ja) |
| HU (1) | HU204897B (ja) |
| IL (1) | IL88322A (ja) |
| NO (1) | NO174110C (ja) |
| NZ (1) | NZ226937A (ja) |
Families Citing this family (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH03242553A (ja) * | 1990-02-19 | 1991-10-29 | Mect Corp | エピシアロ複合糖質を含む製剤 |
| US7682794B2 (en) * | 2003-07-15 | 2010-03-23 | The Regents Of The University Of California | Methods for detecting and analyzing N-glycolylneuraminic acid (Neu5Gc) in biological materials |
| CN100401753C (zh) * | 2004-07-20 | 2008-07-09 | 上海乐金广电电子有限公司 | 数码tv接收用智能天线控制系统 |
| WO2013151649A1 (en) | 2012-04-04 | 2013-10-10 | Sialix Inc | Glycan-interacting compounds |
| US9879087B2 (en) | 2014-11-12 | 2018-01-30 | Siamab Therapeutics, Inc. | Glycan-interacting compounds and methods of use |
| SI3218005T1 (sl) | 2014-11-12 | 2023-06-30 | Seagen Inc. | Z glikanom delujoče spojine, in postopki uporabe |
| CA3002097A1 (en) | 2015-11-12 | 2017-05-18 | Siamab Therapeutics, Inc. | Glycan-interacting compounds and methods of use |
| EP3541847A4 (en) | 2016-11-17 | 2020-07-08 | Seattle Genetics, Inc. | COMPOUNDS INTERACTING WITH GLYCANE AND METHODS OF USE |
| EP3589319A4 (en) | 2017-03-03 | 2021-07-14 | Seagen Inc. | COMPOUNDS INTERACTING WITH GLYCAN AND METHODS OF USE |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS59164798A (ja) * | 1983-03-09 | 1984-09-17 | Rikagaku Kenkyusho | シアル酸含有糖脂質誘導体 |
-
1988
- 1988-02-08 JP JP63026848A patent/JPH02486A/ja active Pending
- 1988-11-08 US US07/268,895 patent/US5158886A/en not_active Expired - Fee Related
- 1988-11-08 KR KR1019880014661A patent/KR960004855B1/ko not_active Expired - Fee Related
- 1988-11-08 IL IL8832288A patent/IL88322A/en not_active IP Right Cessation
- 1988-11-10 CA CA000582783A patent/CA1336763C/en not_active Expired - Fee Related
- 1988-11-10 FI FI885169A patent/FI90989C/fi not_active IP Right Cessation
- 1988-11-11 AU AU24982/88A patent/AU614553B2/en not_active Ceased
- 1988-11-11 HU HU885786A patent/HU204897B/hu not_active IP Right Cessation
- 1988-11-11 NO NO885053A patent/NO174110C/no unknown
- 1988-11-11 NZ NZ226937A patent/NZ226937A/en unknown
- 1988-11-11 EP EP88118876A patent/EP0316818B1/en not_active Expired - Lifetime
- 1988-11-11 ES ES88118876T patent/ES2054772T3/es not_active Expired - Lifetime
- 1988-11-11 DE DE8888118876T patent/DE3881344T2/de not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| JPH02486A (ja) | 1990-01-05 |
| FI90989C (fi) | 1994-04-25 |
| EP0316818B1 (en) | 1993-05-26 |
| NO885053D0 (no) | 1988-11-11 |
| EP0316818A2 (en) | 1989-05-24 |
| KR890007755A (ko) | 1989-07-05 |
| AU2498288A (en) | 1989-05-18 |
| NO885053L (no) | 1989-05-16 |
| NO174110C (no) | 1994-03-16 |
| NZ226937A (en) | 1991-02-26 |
| CA1336763C (en) | 1995-08-22 |
| FI90989B (fi) | 1994-01-14 |
| ES2054772T3 (es) | 1994-08-16 |
| HUT48676A (en) | 1989-06-28 |
| US5158886A (en) | 1992-10-27 |
| DE3881344T2 (de) | 1993-09-09 |
| NO174110B (no) | 1993-12-06 |
| KR960004855B1 (ko) | 1996-04-16 |
| DE3881344D1 (de) | 1993-07-01 |
| FI885169A0 (fi) | 1988-11-10 |
| EP0316818A3 (en) | 1990-08-22 |
| HU204897B (en) | 1992-02-28 |
| FI885169L (fi) | 1989-05-14 |
| AU614553B2 (en) | 1991-09-05 |
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