CN111812330A - Kit for D-dimer detection - Google Patents
Kit for D-dimer detection Download PDFInfo
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- CN111812330A CN111812330A CN202010579300.5A CN202010579300A CN111812330A CN 111812330 A CN111812330 A CN 111812330A CN 202010579300 A CN202010579300 A CN 202010579300A CN 111812330 A CN111812330 A CN 111812330A
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- dimer
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- 239000003154 D dimer Substances 0.000 title claims abstract description 49
- 108010052295 fibrin fragment D Proteins 0.000 title claims abstract description 49
- 238000001514 detection method Methods 0.000 title claims abstract description 14
- 238000004140 cleaning Methods 0.000 claims abstract description 42
- 238000006243 chemical reaction Methods 0.000 claims abstract description 39
- 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 claims abstract description 32
- 230000008878 coupling Effects 0.000 claims abstract description 27
- 238000010168 coupling process Methods 0.000 claims abstract description 27
- 238000005859 coupling reaction Methods 0.000 claims abstract description 27
- 239000007788 liquid Substances 0.000 claims abstract description 17
- 229960002685 biotin Drugs 0.000 claims abstract description 16
- 235000020958 biotin Nutrition 0.000 claims abstract description 16
- 239000011616 biotin Substances 0.000 claims abstract description 16
- 230000001681 protective effect Effects 0.000 claims abstract description 13
- 108090000790 Enzymes Proteins 0.000 claims abstract description 11
- 102000004190 Enzymes Human genes 0.000 claims abstract description 11
- 150000001875 compounds Chemical class 0.000 claims abstract description 9
- 238000005406 washing Methods 0.000 claims abstract description 6
- 239000003085 diluting agent Substances 0.000 claims abstract description 4
- 239000000126 substance Substances 0.000 claims abstract description 4
- 239000000758 substrate Substances 0.000 claims abstract description 4
- 239000000243 solution Substances 0.000 claims description 40
- 239000008055 phosphate buffer solution Substances 0.000 claims description 12
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 claims description 10
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 claims description 8
- 238000001976 enzyme digestion Methods 0.000 claims description 8
- 108010004032 Bromelains Proteins 0.000 claims description 6
- 239000004365 Protease Substances 0.000 claims description 6
- 108090000631 Trypsin Proteins 0.000 claims description 6
- 102000004142 Trypsin Human genes 0.000 claims description 6
- 235000019835 bromelain Nutrition 0.000 claims description 6
- PFKFTWBEEFSNDU-UHFFFAOYSA-N carbonyldiimidazole Chemical compound C1=CN=CN1C(=O)N1C=CN=C1 PFKFTWBEEFSNDU-UHFFFAOYSA-N 0.000 claims description 6
- 229940051841 polyoxyethylene ether Drugs 0.000 claims description 6
- 229920000056 polyoxyethylene ether Polymers 0.000 claims description 6
- 239000012588 trypsin Substances 0.000 claims description 6
- ZORQXIQZAOLNGE-UHFFFAOYSA-N 1,1-difluorocyclohexane Chemical compound FC1(F)CCCCC1 ZORQXIQZAOLNGE-UHFFFAOYSA-N 0.000 claims description 4
- XYZZKVRWGOWVGO-UHFFFAOYSA-N Glycerol-phosphate Chemical compound OP(O)(O)=O.OCC(O)CO XYZZKVRWGOWVGO-UHFFFAOYSA-N 0.000 claims description 4
- 229930006000 Sucrose Natural products 0.000 claims description 4
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 claims description 4
- 238000000034 method Methods 0.000 claims description 4
- 230000008569 process Effects 0.000 claims description 4
- 239000000377 silicon dioxide Substances 0.000 claims description 4
- 235000011069 sorbitan monooleate Nutrition 0.000 claims description 4
- 239000001593 sorbitan monooleate Substances 0.000 claims description 4
- 229940035049 sorbitan monooleate Drugs 0.000 claims description 4
- 239000006224 matting agent Substances 0.000 claims description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 2
- SFNALCNOMXIBKG-UHFFFAOYSA-N ethylene glycol monododecyl ether Chemical compound CCCCCCCCCCCCOCCO SFNALCNOMXIBKG-UHFFFAOYSA-N 0.000 claims description 2
- 239000005720 sucrose Substances 0.000 claims description 2
- 230000035945 sensitivity Effects 0.000 abstract description 4
- 229940088598 enzyme Drugs 0.000 description 7
- 108010073385 Fibrin Proteins 0.000 description 5
- 102000009123 Fibrin Human genes 0.000 description 5
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 5
- 229950003499 fibrin Drugs 0.000 description 5
- 239000008280 blood Substances 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 108010058861 Fibrin Fibrinogen Degradation Products Proteins 0.000 description 3
- 208000007536 Thrombosis Diseases 0.000 description 3
- 239000000208 fibrin degradation product Substances 0.000 description 3
- 235000011187 glycerol Nutrition 0.000 description 3
- 229960004793 sucrose Drugs 0.000 description 3
- 210000004204 blood vessel Anatomy 0.000 description 2
- LQZZUXJYWNFBMV-UHFFFAOYSA-N dodecan-1-ol Chemical compound CCCCCCCCCCCCO LQZZUXJYWNFBMV-UHFFFAOYSA-N 0.000 description 2
- 239000003527 fibrinolytic agent Substances 0.000 description 2
- 230000003480 fibrinolytic effect Effects 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 108090000190 Thrombin Proteins 0.000 description 1
- 230000001476 alcoholic effect Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000020764 fibrinolysis Effects 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000035699 permeability Effects 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 238000004393 prognosis Methods 0.000 description 1
- 235000012239 silicon dioxide Nutrition 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 230000002537 thrombolytic effect Effects 0.000 description 1
- 201000005665 thrombophilia Diseases 0.000 description 1
- 230000017423 tissue regeneration Effects 0.000 description 1
- 230000008733 trauma Effects 0.000 description 1
- 230000002792 vascular Effects 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
- G01N33/6893—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to diseases not provided for elsewhere
-
- 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
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/577—Immunoassay; Biospecific binding assay; Materials therefor involving monoclonal antibodies binding reaction mechanisms characterised by the use of monoclonal antibodies; monoclonal antibodies per se are classified with their corresponding antigens
-
- 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
- G01N33/58—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving labelled substances
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/22—Haematology
- G01N2800/226—Thrombotic disorders, i.e. thrombo-embolism irrespective of location/organ involved, e.g. renal vein thrombosis, venous thrombosis
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/52—Predicting or monitoring the response to treatment, e.g. for selection of therapy based on assay results in personalised medicine; Prognosis
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Chemical & Material Sciences (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Cell Biology (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Food Science & Technology (AREA)
- Medicinal Chemistry (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Microbiology (AREA)
- General Health & Medical Sciences (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Investigating Or Analysing Materials By The Use Of Chemical Reactions (AREA)
Abstract
The invention provides a kit for detecting a D-dimer, and particularly relates to the field of D-dimer detection; comprises compound enzyme liquid, coupling liquid, protective liquid, biotin-labeled D-dimer monoclonal antibody, chemiluminescent substrate, standard substance diluent, washing liquid and a reaction tube; adding 40 microliters of coupling solution into each hole of the reaction tube, incubating for 25min at room temperature, and cleaning the reaction tube for 5 times by using cleaning solution, wherein the cleaning time is 10min each time; adding 150 microliters of biotin-labeled D-dimer monoclonal antibody into each hole of the reaction tube, wherein the coupling temperature is 30 ℃ and the coupling time is 2 hours, and cleaning the reaction tube for 5 times by using cleaning solution, wherein the cleaning time is 10 minutes each time; then adding 80 microliter of protective solution into each hole of the reaction tube, and airing at a ventilated position; the invention can improve the efficiency and sensitivity of detection.
Description
Technical Field
The invention belongs to the field of D-dimer detection, and particularly relates to a kit for detecting D-dimer.
Background
Fibrin exists in blood, and fibrin is activated and hydrolyzed to generate specific degradation products, which are called fibrin degradation products. D-dimer is the simplest fibrin degradation product, and an elevated level of D-dimer indicates the presence of hypercoagulable state and secondary hyperfibrinolysis in vivo. The dynamic balance between the blood coagulation system and the fibrinolysis system in the normal human body is kept, so that the blood circulation can be normally carried out. The fibrinolytic system plays an important role in maintaining normal permeability of the vascular wall, maintaining the flow state of blood, and tissue repair, while the coagulation system forms a thrombus to prevent blood loss from the damaged blood vessel in the case of trauma or damage to the blood vessel. However, in pathological conditions, when the body coagulates blood, thrombin acts on fibrin and is converted into cross-linked fibrin (thrombosis), and the fibrinolytic system is activated (thrombolysis), degrading fibrin to form various fragments, and D-dimer is one of fibrin degradation products. Therefore, the mass concentration of the D-dimer has important significance for the diagnosis, the curative effect evaluation and the prognosis judgment of the thrombotic diseases. However, the sensitivity and detection efficiency of the existing dimer detection still need to be further improved.
Disclosure of Invention
The invention aims to provide a kit for detecting D-dimer, which can improve the detection efficiency and sensitivity.
The invention provides the following technical scheme:
a kit for detecting D-dimer comprises complex enzyme liquid, coupling liquid, protective liquid, biotin-labeled D-dimer monoclonal antibody, chemiluminescent substrate, standard substance diluent, washing liquid and a reaction tube; adding 40 microliters of coupling solution into each hole of the reaction tube, incubating for 25min at room temperature, and cleaning the reaction tube for 5 times by using cleaning solution, wherein the cleaning time is 10min each time; adding 150 microliters of biotin-labeled D-dimer monoclonal antibody into each hole of the reaction tube, wherein the coupling temperature is 30 ℃ and the coupling time is 2 hours, and cleaning the reaction tube for 5 times by using cleaning solution, wherein the cleaning time is 10 minutes each time; and then adding 80 microliter of protective solution into each hole of the reaction tube, and airing at a ventilated place.
Preferably, the biotin-labeled D-dimer monoclonal antibody is composed of 10 mmol/l of a phosphate buffer solution with pH 7.0, 2.0 μ g/mL of a D-dimer antibody, 0.03 mass% of laureth, 1.2 mass% of sucrose, 0.5 mass% of glycerol, and 0.02 mass% of a silica matting agent.
Preferably, 2.0. mu.g/mL of D-dimer antibody is added with 60 microliters of compound enzyme solution through the D-dimer antibody, wherein the enzyme digestion temperature is 38 ℃, and the enzyme digestion process time is 3 hours.
Preferably, the cleaning solution consists of 20 ml of phosphate buffer solution with pH 7.0 and 0.03% of sorbitan monooleate polyoxyethylene ether by mass fraction.
Preferably, the compound enzyme solution consists of trypsin and bromelain, and the mass ratio of the trypsin to the bromelain is 0.6: 0.09.
Preferably, the coupling solution is 2 millimoles per liter of alcoholic solution of N, N' -carbonyldiimidazole; the protective solution adopts 55% of glycerol-phosphate buffer solution by mass fraction.
The invention has the beneficial effects that:
adding 40 microliters of coupling solution into each hole of a reaction tube, incubating for 25min at room temperature, and cleaning the reaction tube for 5 times by using cleaning solution, wherein the cleaning time is 10min each time; adding 150 microliters of biotin-labeled D-dimer monoclonal antibody into each hole of the reaction tube, wherein the coupling temperature is 30 ℃ and the coupling time is 2 hours, and cleaning the reaction tube for 5 times by using cleaning solution, wherein the cleaning time is 10 minutes each time; then adding 80 microliter of protective solution into each hole of the reaction tube, and airing at a ventilated place; the product has high sensitivity, convenient and simple operation, short operation time, low cost, high resistance and strong anti-interference capability, and does not need instruments with high value.
Detailed Description
A kit for detecting D-dimer comprises complex enzyme liquid, coupling liquid, protective liquid, biotin-labeled D-dimer monoclonal antibody, chemiluminescent substrate, standard substance diluent, washing liquid and a reaction tube; adding 40 microliters of coupling solution into each hole of the reaction tube, incubating for 25min at room temperature, and cleaning the reaction tube for 5 times by using cleaning solution, wherein the cleaning time is 10min each time; adding 150 microliters of biotin-labeled D-dimer monoclonal antibody into each hole of the reaction tube, wherein the coupling temperature is 30 ℃ and the coupling time is 2 hours, and cleaning the reaction tube for 5 times by using cleaning solution, wherein the cleaning time is 10 minutes each time; then adding 80 microliter of protective solution into each hole of the reaction tube, and airing at a ventilated position;
example 2:
a kit for detecting D-dimer, wherein the biotin-labeled D-dimer monoclonal antibody consists of 10 millimoles per liter of phosphate buffer solution with the pH value of 7.0, 2.0 mu g/mL of D-dimer antibody, 0.03 mass percent of lauryl alcohol polyoxyethylene ether, 1.2 mass percent of cane sugar, 0.5 mass percent of glycerin and 0.02 mass percent of silica matting agent; adding 2.0 mu g/mL of D-dimer antibody into 60 microliters of compound enzyme solution through the D-dimer antibody, wherein the enzyme digestion temperature is 38 ℃, and the enzyme digestion process time is 3 hours; adding 40 microliters of coupling solution into each hole of the reaction tube, incubating for 25min at room temperature, and cleaning the reaction tube for 5 times by using cleaning solution, wherein the cleaning time is 10min each time; adding 150 microliters of biotin-labeled D-dimer monoclonal antibody into each hole of the reaction tube, wherein the coupling temperature is 30 ℃ and the coupling time is 2 hours, and cleaning the reaction tube for 5 times by using cleaning solution, wherein the cleaning time is 10 minutes each time; then adding 80 microliter of protective solution into each hole of the reaction tube, and airing at a ventilated position;
example 3:
a kit for detecting D-dimer, which comprises biotin-labeled D-dimer monoclonal antibody, a probe and a probe, wherein the biotin-labeled D-dimer monoclonal antibody consists of 10 millimoles per liter of phosphate buffer solution with the pH value of 7.0, 2.0 mu g/mL of D-dimer antibody, 0.03 mass percent of lauryl alcohol polyoxyethylene ether, 1.2 mass percent of cane sugar, 0.5 mass percent of glycerin and 0.02 mass percent of silicon dioxide delustering agent; adding 2.0 mu g/mL of D-dimer antibody into 60 microliters of compound enzyme solution through the D-dimer antibody, wherein the enzyme digestion temperature is 38 ℃, and the enzyme digestion process time is 3 hours; the cleaning solution consists of 20 ml of phosphate buffer solution with the pH value of 7.0 and 0.03 percent of sorbitan monooleate polyoxyethylene ether; the compound enzyme solution consists of trypsin and bromelain, and the mass ratio of the trypsin to the bromelain is 0.6: 0.09; the coupling solution is 2 millimoles per liter of alcohol solution of N, N' -carbonyldiimidazole; the protective solution adopts 55 mass percent of glycerol-phosphate buffer solution; adding 40 microliters of coupling solution into each hole of the reaction tube, incubating for 25min at room temperature, and cleaning the reaction tube for 5 times by using cleaning solution, wherein the cleaning time is 10min each time; adding 150 microliters of biotin-labeled D-dimer monoclonal antibody into each hole of the reaction tube, coupling at 30 ℃ for 2 hours, and washing the reaction tube for 5 times by using 20 milliliters of phosphate buffer solution with the pH value of 7.0 and sorbitan monooleate polyoxyethylene ether with the mass fraction of 0.03 percent, wherein the washing time is 10 minutes each time; adding 80 microliters of glycerol-phosphate buffer solution with the mass fraction of 55% into each hole of the reaction tube, and airing at a ventilated place;
although the present invention has been described in detail with reference to the foregoing embodiments, those skilled in the art will understand that various changes, modifications and substitutions can be made without departing from the spirit and scope of the invention as defined by the appended claims. Any modification, equivalent replacement, or improvement made within the spirit and principle of the present invention should be included in the protection scope of the present invention.
Claims (6)
1. A kit for D-dimer detection, characterized in that: comprises compound enzyme liquid, coupling liquid, protective liquid, biotin-labeled D-dimer monoclonal antibody, chemiluminescent substrate, standard substance diluent, washing liquid and a reaction tube; adding 40 microliters of coupling solution into each hole of the reaction tube, incubating for 25min at room temperature, and cleaning the reaction tube for 5 times by using cleaning solution, wherein the cleaning time is 10min each time; adding 150 microliters of biotin-labeled D-dimer monoclonal antibody into each hole of the reaction tube, wherein the coupling temperature is 30 ℃ and the coupling time is 2 hours, and cleaning the reaction tube for 5 times by using cleaning solution, wherein the cleaning time is 10 minutes each time; and then adding 80 microliter of protective solution into each hole of the reaction tube, and airing at a ventilated place.
2. A kit for D-dimer detection according to claim 1, characterized in that: the biotin-labeled D-dimer monoclonal antibody was composed of 10 mmol/l of a phosphate buffer solution having a pH of 7.0, 2.0 μ g/mL of a D-dimer antibody, 0.03% by mass of laureth, 1.2% by mass of sucrose, 0.5% by mass of glycerol, and 0.02% by mass of a silica matting agent.
3. A kit for D-dimer detection according to claim 1, characterized in that: adding 60 microliters of compound enzyme liquid into 2.0 micrograms/mL of D-dimer antibody through the D-dimer antibody, wherein the enzyme digestion temperature is 38 ℃, and the enzyme digestion process time is 3 hours.
4. A kit for D-dimer detection according to claim 1, characterized in that: the cleaning solution consists of 20 ml of phosphate buffer solution with the pH value of 7.0 and 0.03 percent of sorbitan monooleate polyoxyethylene ether by mass fraction.
5. A kit for D-dimer detection according to claim 1, characterized in that: the compound enzyme solution consists of trypsin and bromelain, and the mass ratio of the trypsin to the bromelain is 0.6: 0.09.
6. A kit for D-dimer detection according to claim 1, characterized in that: the coupling solution is 2 millimoles per liter of alcohol solution of N, N' -carbonyldiimidazole; the protective solution adopts 55% of glycerol-phosphate buffer solution by mass fraction.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202010579300.5A CN111812330A (en) | 2020-06-23 | 2020-06-23 | Kit for D-dimer detection |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202010579300.5A CN111812330A (en) | 2020-06-23 | 2020-06-23 | Kit for D-dimer detection |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN111812330A true CN111812330A (en) | 2020-10-23 |
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202010579300.5A Pending CN111812330A (en) | 2020-06-23 | 2020-06-23 | Kit for D-dimer detection |
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| Country | Link |
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| CN (1) | CN111812330A (en) |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107247138A (en) * | 2017-07-21 | 2017-10-13 | 王贤俊 | The method for coating of Chemiluminescent plate in a kind of measure D dimer contents |
| CN107462732A (en) * | 2017-07-21 | 2017-12-12 | 王贤俊 | The method for coating of Chemiluminescent plate in a kind of measure saccharification hemoglobin content |
| CN109444412A (en) * | 2018-10-26 | 2019-03-08 | 成都普利泰生物科技有限公司 | A kind of pet d-dimer detection kit for very small chemical luminescence immunoassay system |
| WO2019184248A1 (en) * | 2018-03-27 | 2019-10-03 | 苏州长光华医生物医学工程有限公司 | Adamantane chemiluminescence kit for detecting force growth factor and e-peptide thereof, and preparation method |
| CN111007250A (en) * | 2019-12-10 | 2020-04-14 | 江苏三联生物工程有限公司 | Electrochemiluminescence kit for detecting TAT (thrombin-antithrombin complex) and preparation method |
-
2020
- 2020-06-23 CN CN202010579300.5A patent/CN111812330A/en active Pending
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107247138A (en) * | 2017-07-21 | 2017-10-13 | 王贤俊 | The method for coating of Chemiluminescent plate in a kind of measure D dimer contents |
| CN107462732A (en) * | 2017-07-21 | 2017-12-12 | 王贤俊 | The method for coating of Chemiluminescent plate in a kind of measure saccharification hemoglobin content |
| WO2019184248A1 (en) * | 2018-03-27 | 2019-10-03 | 苏州长光华医生物医学工程有限公司 | Adamantane chemiluminescence kit for detecting force growth factor and e-peptide thereof, and preparation method |
| CN109444412A (en) * | 2018-10-26 | 2019-03-08 | 成都普利泰生物科技有限公司 | A kind of pet d-dimer detection kit for very small chemical luminescence immunoassay system |
| CN111007250A (en) * | 2019-12-10 | 2020-04-14 | 江苏三联生物工程有限公司 | Electrochemiluminescence kit for detecting TAT (thrombin-antithrombin complex) and preparation method |
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Application publication date: 20201023 |
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| RJ01 | Rejection of invention patent application after publication |