EP1152242A1 - Behälter für immunoassays - Google Patents
Behälter für immunoassays Download PDFInfo
- Publication number
- EP1152242A1 EP1152242A1 EP99951118A EP99951118A EP1152242A1 EP 1152242 A1 EP1152242 A1 EP 1152242A1 EP 99951118 A EP99951118 A EP 99951118A EP 99951118 A EP99951118 A EP 99951118A EP 1152242 A1 EP1152242 A1 EP 1152242A1
- Authority
- EP
- European Patent Office
- Prior art keywords
- container
- polymer
- adsorption
- molecules
- solution
- 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.)
- Granted
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Classifications
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01L—CHEMICAL OR PHYSICAL LABORATORY APPARATUS FOR GENERAL USE
- B01L3/00—Containers or dishes for laboratory use, e.g. laboratory glassware; Droppers
- B01L3/50—Containers for the purpose of retaining a material to be analysed, e.g. test tubes
Definitions
- the present invention relates to a container used for storage, dilution, or reaction of a reagent and/or a test sample, in an immunoassay for detecting an antigen or an antibody through antigen-antibody reaction.
- samples used for clinical diagnosis such as serum and urine
- samples used for clinical diagnosis such as serum and urine
- samples used for clinical diagnosis are collected from patients, placed in a container, and stored therein until the samples are subjected to assay
- clinically important proteins contained in the samples such as albumin, transferrin, and immunoglobulin
- Most containers used for clinical diagnosis including syringes and cups used in the step of collecting a sample, tubes used in the step of storing the sample, and centrifugation tubes and test tubes used in the step of purifying, concentrating, or diluting the sample, are formed from polypropylene or polystyrene, and such a container is not subjected to surface treatment. Therefore, when even a trace amount of proteins contained in the sample is adsorbed onto the container in each step, the concentration of the proteins is expected to vary greatly after all the steps have been performed, as compared with the concentration of the proteins at the time of collection of the sample.
- the price of a reagent in immobilized form accounts for about 80% the cost of a clinical test kit sold by a clinical test drug manufacturer. Therefore, when reduction in the reagent due to adsorption onto a container is suppressed, production costs are greatly reduced.
- a solid phase method (a type of immunoassay method) assay is carried out by utilizing proteins immobilized onto the surface of a container for an immunoassay. Therefore, a solid phase method employs a container subjected to "high adsorption treatment," in which, in order to increase the amount of a reagent which is to be immobilized onto the surface of the container, a hydrophilic-hydrophobic balance of the surface is regulated through introduction of a functional group such as a hydroxyl group, thereby increasing the saturation adsorption amount of the reagent.
- high adsorption treatment in which, in order to increase the amount of a reagent which is to be immobilized onto the surface of the container, a hydrophilic-hydrophobic balance of the surface is regulated through introduction of a functional group such as a hydroxyl group, thereby increasing the saturation adsorption amount of the reagent.
- a container used for such a method is provided without consideration of molecular adsorption; i.e., the container is formed from polystyrene or polypropylene in consideration of only shapability, transparency, and low-temperature resistance, and the container is not subjected to surface treatment for suppressing adsorption of molecules. From the viewpoint of characteristics of the container, no attempt has been made to solve problems such as loss of a reagent and reduction in sensitivity.
- a blocking method is most widely carried out, in which a container is coated with a protein inactive to a sample which is to be assayed. Since the method basically utilizes non-specific adsorption of the protein onto the container, blocking effects may differ from container to container, and may depend on the state of the protein. In addition, since the inactive protein is non-specifically adsorbed onto the container, the protein is easily detached from the container into a solution, and thus the container cannot be used for storing the solution.
- Japanese Patent Application Laid-Open ( kokai ) Nos. 6-174726 and 7-128336 disclose a technique in which such detachment of a protein is eliminated by chemically immobilizing the protein onto a container.
- the structure of the protein may vary in accordance with drying temperature, storage temperature, and storage time, and thus the container is not widely used in practice.
- the protein When the higher-order structure of a protein adsorbed onto a container varies, the protein induces secondary adsorption.
- the protein When a protein which is inactive in a free state is adsorbed onto or chemically bound to a container, the protein cannot completely maintain its inactive state, due to alteration of the higher-order structure. Therefore, even when adsorption of another protein onto the container can be prevented, variance of the higher-order structure induces secondary adsorption between the proteins.
- the present inventors have performed extensive studies on characteristics of a container, and have found that when the saturation amount of molecules which are adsorbed onto the container, the molecules being used for an immunoassay, is controlled to a predetermined value or less, loss of a reagent or a sample is prevented during storage, dilution, and reaction, and the sample can be assayed at high sensitivity.
- the present invention has been accomplished on the basis of this finding.
- the present invention provides a container for an immunoassay in which the saturation adsorption amount of molecules used for the assay is 1 ⁇ 10 -1 pmol/cm 2 or less.
- the adsorption amount of molecules is about 1-10 pmol/cm 2 or more; i.e., about 20-50% of molecules (e.g., proteins) used for an immunoassay are adsorbed onto the container, although the adsorption amount varies in accordance with the concentration of a solution containing such molecules and the contact area between the molecules and the container.
- the adsorbed molecules (20-50% of all the molecules) are essential for reaction in the solution, reaction efficiency; i.e., assay sensitivity, is reduced by 20-50%. Meanwhile, when the adsorbed substance is such that it undergoes molecular structural changes due to adsorption to thereby cause unwanted reaction, considerable noise would result.
- the container desirably meets the following conditions: the saturation adsorption amount of the molecules used in the immunoassay is 1 ⁇ 10 -1 pmol/cm 2 or less under the specific conditions ⁇ in terms of concentration of the solution, temperature, and pH of the solvent ⁇ under which the reaction and assay are carried out.
- the effect of the invention can be attained if the saturation adsorption amount of the molecules which participate in and/or affect the assay, among all molecules contained in the diluted serum, is always 1 ⁇ 10 -1 pmol/cm 2 or less at the diluted concentration of serum and under the specific conditions ⁇ in terms of concentration of the solution, temperature, and pH of the solvent ⁇ under which the reaction and assay are carried out.
- the effect of the invention can be attained if the saturation adsorption amount of the molecules that undergo storage and dilution is always 1 ⁇ 10 -1 pmol/cm 2 or less under the specific conditions ⁇ in terms of concentration of the solution, temperature, and pH of the solvent ⁇ under which the reagent is removed from the storage container or dilution is carried out.
- the reagent is stored in the container at a temperature as low as -80°C.
- the saturation adsorption amount of molecules is 1 ⁇ 10 -1 pmol/cm 2 or less under the specific conditions ⁇ in terms of concentration, temperature, and pH ⁇ under which the reagent is removed from the container.
- the saturation adsorption amount of the molecules is more preferably 1 ⁇ 10 -2 pmol/cm 2 or less, much more preferably 1 ⁇ 10 -3 pmol/cm 2 or less.
- proteins e.g., enzymes, physiologically active proteins, and antibodies
- nucleic acids e.g., glucose, and glutathione
- physiologically active substances e.g., glucose, and others.
- proteins e.g., enzymes, physiologically active proteins, and antibodies
- nucleic acids e.g., amino acids, amino acids, and amino acids.
- physiologically active substances e.g., amino acids, amino acids, and antibodies
- nucleic acids e.g., amino acids, amino acids, and physiologically active substances.
- physiologically active substances e.g., amino acids, amino acids, amino acids, and others.
- physiologically active substances e.g., amino acids, amino acids, and others.
- the saturation adsorption amount of the molecules can be measured by means of colloidal gold labeling immunoassay.
- the present invention exerts excellent effects in addition to the aforementioned characteristic feature.
- a protein is adsorbed onto a container, the structure of the protein is varied. Therefore, when an immunoassay is carried out, although a target protein is contained in a sample to be assayed, the protein may fail to be detected by an antibody, due to variation in the structure of the protein.
- serum whose structure has been altered due to adsorption is assayed, even though serum must be assayed in the same state in which the serum is present in an organism.
- the container of the present invention since a protein is not adsorbed onto the container, the structure of the protein is not altered, and thus when a clinical test is carried out by use of the container, serum can be assayed in a state similar to that in which serum is present in an organism. Therefore, the container of the present invention is very advantageously used as a container for an immunoassay.
- the saturation adsorption amount of molecules In a container for an immunoassay, the saturation adsorption amount of molecules must be decreased at a portion with which a reagent or a sample is brought into contact; specifically, an inner surface of the container. Therefore, the molecular saturation adsorption amount at an inner surface of the container should be at least 1 ⁇ 10 -1 pmol/cm 2 or less.
- At least the inner surface is formed from a highly hydrophilic polymer or a highly hydrophobic polymer, or is coated with a highly hydrophilic polymer or a highly hydrophobic polymer. More preferably, at least the inner surface is coated with a highly hydrophilic polymer or a highly hydrophobic polymer. Much more preferably, at least the inner surface is coated with a highly hydrophilic polymer. Particularly preferably, at least the inner surface is coated with an ultra-hydrophilic polymer.
- highly hydrophobic polymers include fluorine-containing resins such as polytetrafluoroethylene (PTFE) and silicon-containing resins.
- PTFE polytetrafluoroethylene
- the surface of the container is coated with a hydrophobic polymer, the surface may be coated with the aforementioned hydrophobic polymer, or the container may be fluorinated, thereby forming a fluorinated polymer film on the surface thereof.
- hydrophilic polymer No particular limitation is imposed on the highly hydrophilic polymer, so long as the polymer contains a hydrophilic group such as a carboxyl group or a hydroxyl group.
- hydrophilic polymer examples include polymethacrylic acid, (meth)methacrylic acid-alkyl methacrylate copolymers, polyhydroxyalkyl methacrylates (e.g., polyhydroxyethyl methacrylate), hydroxyalkyl methacrylate-alkyl methacrylate copolymers, polyoxyalkylene-group-containing methacrylate polymer and copolymers containing the polymer, polyvinyl pyrrolidone, ethylene-vinyl alcohol copolymers, (2-methacryloyloxyethylphosphocholine) polymers (MPC) and copolymers containing the polymers (Seitai Zairyo, Vol.
- the container may be formed from such a hydrophilic polymer, or coated with the polymer.
- a hydroxyl group or a carboxyl group may be introduced into the surface of the container, to thereby impart high hydrophilicity; i.e., low adsorbability, to the surface of the container.
- a surface exhibiting low adsorbability can be realized by means of surface modification.
- the container is formed from a material which tends to induce non-specific adsorption, such as polystyrene or polypropylene, a carboxyl group, a carbonyl group, and/or a hydroxyl group may be introduced into the surface of the container through plasma exposure, to thereby impart low adsorbability to the surface.
- a carboxyl group may be introduced into the surface of the container through partial hydrolysis of the surface by use of an alkali, to thereby impart low adsorbability to the surface.
- the contact angle between the surface and water is preferably 30° or less (highly hydrophilic), more preferably 15° or less, much more preferably 1° or less (ultra-hydrophilic).
- hydrophilic polymers there is employed a polyhydroxyalkyl methacrylate, a polyoxy (C 2 -C 4 alkylene-group-containing methacrylate) polymer or a copolymer containing the polymer; a (2-methacryloyloxyethylphosphocholine) polymer or a copolymer containing the polymer; a phospholipid.polymer composite; or polyvinyl pyrrolidone
- the contact angle between the surface of the resultant container and water becomes 1° or less (i.e., the container is ultra-hydrophilic), and the saturation adsorption amount of proteins becomes 1 ⁇ 10 -3 pmol/cm 2 or less, which is particularly preferable.
- the product form of the container of the present invention is not particularly limited, and the container may assume conventionally used product forms, including a sample tube, a centrifugation tube, a multi-well plate, and a cuvette. However, in order to carry out storage, dilution, reaction, and assay of a sample in one container, the container preferably assumes a form of multi-well plate.
- a commercially available polypropylene-made 96-well plate (MS-3396P, product of Sumitomo Bakelite Co., Ltd.) was subjected to ⁇ -ray treatment at 70 kGy, to thereby generate a hydroxyl group on the surface of the plate.
- the saturation adsorption amount of proteins was 4.6 ⁇ 10 -2 pmol/cm 2
- the contact angle between the surface and the water was 27°.
- a commercially available polypropylene-made 96-well plate (MS-3396P, product of Sumitomo Bakelite Co., Ltd.) was coated with a commercially available fluorine-containing coating agent (Scotchguard, product of Sumitomo 3M Ltd.).
- the saturation adsorption amount of proteins was 2.7 ⁇ 10 -2 pmol/cm 2
- the contact angle between the surface and the water was 126°.
- a commercially available polypropylene-made 96-well plate (MS-3396P, product of Sumitomo Bakelite Co., Ltd.) was used as a comparative plate.
- the saturation adsorption amount of proteins was 3.7 pmol/cm 2
- the contact angle between the surface and the water was 92°.
- solutions of an enzyme-labeled anti-bovine-albumin antibody (product of Cosmo Bio) were prepared (concentration of the antibody: 0.1 ng/mL, 1 ng/mL, 10 ng/mL, and 100 ng/mL, respectively); each solution was injected into 24 wells of each of the plates of Examples 1 and 2 and Comparative Example 1; the plate was stored at -80°C for 48 hours; and after storage time had elapsed, the concentration of the protein in each solution was measured by use of a substrate solution.
- an enzyme-labeled anti-bovine-albumin antibody product of Cosmo Bio
- Rat albumin (product of Cosmo Bio) was dissolved in a phosphate buffer (Dulbecco PBS pH 7.4) to thereby prepare solutions (concentration of the albumin: 10 ng/mL, 1 ng/mL, and 0.1 ng/mL, respectively), and each solution was injected into four lines (i.e., 32 wells) (100 ⁇ l per well) of each of the plates of Examples 1 and 2 and Comparative Example 1.
- the results are shown in Fig. 2.
- the results show that, in relation to the plate of Comparative Example 1, the absorbance is low when the concentration of the albumin is low; i.e., the reaction in the solution is impeded due to adsorption, and that, in relation to the plates of Examples 1 and 2, linearity is obtained between the concentration of the albumin and the absorbance when the albumin concentration is low; i.e., the antigen-antibody reaction in the solution is efficiently carried out.
- a commercially available polystyrene-made tube (Eiken tube for RIA No. 3, 70-12458) was coated with polyhydroxyethyl methacrylate (P-3932, product of SIGMA).
- P-3932 polyhydroxyethyl methacrylate
- the saturation adsorption amount of proteins was 9.1 ⁇ 10 -4 pmol/cm 2
- the contact angle between the surface and the water was 0°.
- Polytetrafluoroethylene was formed into a tube of the same inner diameter and volume as the tube of Example 1.
- the saturation adsorption amount of proteins was 7.2 ⁇ 10 -3 pmol/cm 2
- the contact angle between the surface and the water was 126°.
- a commercially available polystyrene-made tube (Eiken tube for RIA No. 3, 70-12458) was used as a comparative tube.
- the saturation adsorption amount of proteins was 8.1 pmol/cm 2
- the contact angle between the surface and the water was 85°.
- Phosphate buffer (pH 7.4) solutions of biotin hydrazide (product of Dojindo) were prepared in advance (concentration of biotin hydrazide: 0.125 ⁇ g/mL, 0.250 ⁇ g/mL, and 0.500 ⁇ g/mL, respectively).
- biotin hydrazide was immobilized onto ELISA balls (amino-group-containing ball, product of Sumitomo Bakelite Co., Ltd.) through covalent bonding via glutaraldehyde, to thereby prepare ELISA balls having three different immobilization densities of biotin hydrazide.
- Example 4 Each of the above-prepared ELISA balls was placed into each of the tubes of Example 3, Example 4, and Comparative Example 2 (three tubes for each Example), a phosphate buffer (pH 7.4) solution of peroxydase-labeled avidin (product of Cappel) (concentration of avidin: 1 ⁇ g/mL) was injected into each tube (500 mL per tube), and reaction was carried out in each tube at room temperature for 30 minutes.
- a phosphate buffer (pH 7.4) solution of peroxydase-labeled avidin product of Cappel
- concentration of avidin 1 ⁇ g/mL
- solutions of an enzyme-labeled anti-bovine-albumin antibody (product of Cosmo Bio) were prepared (concentration of the antibody: 0.1 ng/mL, 1 ng/mL, 10 ng/mL, and 100 ng/mL, respectively); each solution was injected into 24 wells of each of the plate of Example 3, the plate of Example 4, and the plate of Comparative Example 2; the plates were stored at -80°C for 48 hours; and after storage time had elapsed, the concentration of the protein in each solution was measured by use of a substrate solution.
- an enzyme-labeled anti-bovine-albumin antibody product of Cosmo Bio
- MPC-BMA butyl methacrylate copolymer
- a commercially available polystyrene-made tube (Eiken tube for RIA No. 3, 70-12458) was used in "as is” form as a comparative tube.
- Phosphate buffer (pH 7.4) solutions of biotin hydrazide (product of Dojindo) were prepared in advance (concentration of biotin hydrazide: 0.125 ⁇ g/mL, 0.250 ⁇ g/mL, and 0.500 ⁇ g/mL).
- concentration of biotin hydrazide 0.125 ⁇ g/mL, 0.250 ⁇ g/mL, and 0.500 ⁇ g/mL.
- biotin hydrazide was immobilized onto ELISA balls through covalent bonding via glutaraldehyde, to thereby prepare ELISA balls having three different immobilization densities of biotin hydrazide.
- Example 5 Each of the above-prepared ELISA balls was placed into the tubes of Example 5, Example 6, and Comparative Example 3 (three tubes for each Example), a phosphate buffer (pH 7.4) solution of peroxydase-labeled avidin (product of Cappel) (concentration of avidin: 1 ⁇ g/mL) was injected into each tube (500 mL per tube), and reaction was carried out at room temperature for 30 minutes.
- a phosphate buffer (pH 7.4) solution of peroxydase-labeled avidin product of Cappel
- concentration of avidin 1 ⁇ g/mL
- solutions of an enzyme-labeled anti-bovine-albumin antibody (product of Cosmo Bio) were prepared (concentration of the antibody: 0.1 ng/mL, 1 ng/mL, 10 ng/mL, and 100 ng/mL); each solution was injected into 24 wells of each plate; the plates were stored at -80°C for 48 hours; and after storage was completed, the concentration of the protein in each solution was measured by use of a substrate solution.
- the adsorption amount of molecules or serum used for the assay is 1 ⁇ 10 -1 pmol/cm 2 or less, and thus loss of a reagent, which is caused by adsorption, is prevented during storage or dilution of the reagent. Therefore, when the container is used for a liquid-phase reaction, an assay can be carried out at high sensitivity and high accuracy, since there is prevented decrease in reaction efficiency, which is caused by adsorption of molecules to be assayed, or impediment of reaction due to adsorption of unwanted molecules.
- the test can be carried out under conditions similar to those inside the body of an organism, since variation of the structure of serum components, which is caused by adsorption, does not occur in the container.
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- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Analytical Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Hematology (AREA)
- Clinical Laboratory Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Automatic Analysis And Handling Materials Therefor (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
- Heterocyclic Compounds That Contain Two Or More Ring Oxygen Atoms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (7)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP36740498 | 1998-12-24 | ||
| JP36740498 | 1998-12-24 | ||
| JP5625399 | 1999-03-03 | ||
| JP5625399 | 1999-03-03 | ||
| JP21209699 | 1999-07-27 | ||
| JP21209699 | 1999-07-27 | ||
| PCT/JP1999/005979 WO2000039582A1 (en) | 1998-12-24 | 1999-10-28 | Container for immunologic assay |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| EP1152242A1 true EP1152242A1 (de) | 2001-11-07 |
| EP1152242A4 EP1152242A4 (de) | 2002-03-06 |
| EP1152242B1 EP1152242B1 (de) | 2005-12-28 |
Family
ID=27295858
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EP99951118A Expired - Lifetime EP1152242B1 (de) | 1998-12-24 | 1999-10-28 | Behälter für immunoassays |
Country Status (7)
| Country | Link |
|---|---|
| EP (1) | EP1152242B1 (de) |
| JP (1) | JP3681983B2 (de) |
| AT (1) | ATE314147T1 (de) |
| AU (1) | AU6366799A (de) |
| CA (1) | CA2356857A1 (de) |
| DE (1) | DE69929248T2 (de) |
| WO (1) | WO2000039582A1 (de) |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7648833B2 (en) * | 2003-06-25 | 2010-01-19 | Nof Corporation | Container for germ layer formation and method of forming germ layer |
| CN109153882A (zh) * | 2016-05-24 | 2019-01-04 | 公益财团法人癌研究会 | 细胞外小泡回收方法及细胞外小泡用容器 |
| US11470841B2 (en) | 2016-06-15 | 2022-10-18 | Nissan Chemical Corporation | Cryopreservation vessel |
| US12291701B2 (en) | 2017-09-26 | 2025-05-06 | Nissan Chemical Corporation | Cell culture container having minute volume |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE10356752A1 (de) | 2003-12-04 | 2005-06-30 | Roche Diagnostics Gmbh | Beschichtete Testelemente |
| US20110177955A1 (en) * | 2004-10-12 | 2011-07-21 | Luis Alberto Burzio | Multiplexed protein adsorption assay |
| JP2009050201A (ja) * | 2007-08-27 | 2009-03-12 | Dainippon Printing Co Ltd | 初期胚等用培養器具 |
| JP6866298B2 (ja) * | 2015-11-24 | 2021-04-28 | Jsr株式会社 | 多孔質粒子の製造方法、多孔質粒子、担体、カラム、及び標的物質の分離方法 |
| EP3882627B1 (de) * | 2018-11-14 | 2024-07-10 | Nissan Chemical Corporation | Behälter und verfahren zum lagern, vorbehandeln und analysieren von biomaterial |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| BE789839A (fr) * | 1971-10-08 | 1973-02-01 | Ceskoslovenska Akademie Ved | Procede pour le traitement superficiel d'articles |
| US4472357A (en) * | 1981-11-18 | 1984-09-18 | Medical Laboratory Automation, Inc. | Blood bank cuvette cassette and label therefor |
| FI833207A0 (fi) * | 1983-09-08 | 1983-09-08 | Farmos Oy | Reaktionskaerl foer immunologiska bestaemningar |
| JPS6091983A (ja) * | 1983-10-25 | 1985-05-23 | Susumu Kogyo Kk | タンパク質固定用膜担体およびその製造方法 |
| JPH0419561A (ja) * | 1990-05-14 | 1992-01-23 | Nippon Shokubai Co Ltd | 免疫アッセイ用ブロッキング剤 |
| JPH0833472A (ja) * | 1994-07-25 | 1996-02-06 | Terumo Corp | 細胞リザーバー |
| JP3884510B2 (ja) * | 1996-10-14 | 2007-02-21 | 日本油脂株式会社 | 固定化免疫学的活性物質の保存時安定化方法 |
-
1999
- 1999-10-28 EP EP99951118A patent/EP1152242B1/de not_active Expired - Lifetime
- 1999-10-28 AT AT99951118T patent/ATE314147T1/de not_active IP Right Cessation
- 1999-10-28 CA CA002356857A patent/CA2356857A1/en not_active Abandoned
- 1999-10-28 AU AU63667/99A patent/AU6366799A/en not_active Abandoned
- 1999-10-28 JP JP2000591430A patent/JP3681983B2/ja not_active Expired - Fee Related
- 1999-10-28 WO PCT/JP1999/005979 patent/WO2000039582A1/ja not_active Ceased
- 1999-10-28 DE DE69929248T patent/DE69929248T2/de not_active Expired - Lifetime
Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7648833B2 (en) * | 2003-06-25 | 2010-01-19 | Nof Corporation | Container for germ layer formation and method of forming germ layer |
| US8278097B2 (en) | 2003-06-25 | 2012-10-02 | Nof Corporation | Method for forming embryoid bodies |
| CN109153882A (zh) * | 2016-05-24 | 2019-01-04 | 公益财团法人癌研究会 | 细胞外小泡回收方法及细胞外小泡用容器 |
| US10955410B2 (en) | 2016-05-24 | 2021-03-23 | Japanese Foundation For Cancer Research | Method of recovering extracellular vesicles and container for extracellular vesicles |
| CN109153882B (zh) * | 2016-05-24 | 2022-03-04 | 公益财团法人癌研究会 | 细胞外小泡回收方法及细胞外小泡用容器 |
| US11470841B2 (en) | 2016-06-15 | 2022-10-18 | Nissan Chemical Corporation | Cryopreservation vessel |
| US12291701B2 (en) | 2017-09-26 | 2025-05-06 | Nissan Chemical Corporation | Cell culture container having minute volume |
Also Published As
| Publication number | Publication date |
|---|---|
| EP1152242B1 (de) | 2005-12-28 |
| CA2356857A1 (en) | 2000-07-06 |
| DE69929248D1 (de) | 2006-02-02 |
| WO2000039582A1 (en) | 2000-07-06 |
| DE69929248T2 (de) | 2006-08-17 |
| AU6366799A (en) | 2000-07-31 |
| EP1152242A4 (de) | 2002-03-06 |
| ATE314147T1 (de) | 2006-01-15 |
| JP3681983B2 (ja) | 2005-08-10 |
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