CN113671197B - Buffer solution, calibrator, kit, preparation method and application - Google Patents
Buffer solution, calibrator, kit, preparation method and application Download PDFInfo
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- CN113671197B CN113671197B CN202110955209.3A CN202110955209A CN113671197B CN 113671197 B CN113671197 B CN 113671197B CN 202110955209 A CN202110955209 A CN 202110955209A CN 113671197 B CN113671197 B CN 113671197B
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- 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
- G01N33/74—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving hormones or other non-cytokine intercellular protein regulatory factors such as growth factors, including receptors to hormones and growth factors
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- 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
- G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
- G01N33/54313—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals the carrier being characterised by its particulate form
- G01N33/54326—Magnetic particles
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- 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
- G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
- G01N33/54393—Improving reaction conditions or stability, e.g. by coating or irradiation of surface, by reduction of non-specific binding, by promotion of specific binding
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- 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
- 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
- G01N2333/575—Hormones
- G01N2333/58—Atrial natriuretic factor complex; Atriopeptin; Atrial natriuretic peptide [ANP]; Brain natriuretic peptide [BNP, proBNP]; Cardionatrin; Cardiodilatin
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- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2496/00—Reference solutions for assays of biological material
- G01N2496/45—Reference solutions for assays of biological material containing protease inhibitors, e.g. sulfonylfluorides, chloromethylketones, organophosphates
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Abstract
In order to solve the technical problem that the sample detection has deviation due to poor stability of a calibrator in the existing kit for measuring the B-type natriuretic peptide, the embodiment of the invention provides a buffer solution, a calibrator, a kit, a preparation method and application. The buffer solution is a buffer solution containing a papain inhibitor and aprotinin. The calibrator is a mixture of the buffer and BNP antigen. Use of a buffer or calibrator for determining type B natriuretic peptide. A kit for determining type B natriuretic peptide comprising: the calibrator. The preparation method of the buffer solution comprises the following steps: the bovine serum albumin, PC-950, tween-20, papain inhibitor and aprotinin are added into Tris-HCl buffer solution to prepare the kit. The papain inhibitor and the aprotinin are added into the buffer solution, so that degradation of BNP antigen can be inhibited and inhibited during use, stability of a calibrator is improved, and accuracy of a detection sample of the kit in clinical application is improved to a certain extent.
Description
Technical Field
The invention relates to a buffer solution, a calibrator, a kit, a preparation method and application.
Background
Type B Natriuretic Peptide (BNP), also known as brain natriuretic peptide, is a hormone secreted by the heart and brain. Has the main functions of regulating body fluid, promoting urination, regulating sodium balance in human body, resisting aldosterone, dilating blood vessel and regulating blood pressure. Brain natriuretic peptides are secreted mainly by cardiomyocytes, and their 108 amino acid precursors (ProBNP) can be broken down into a biologically active 32 amino acid C-terminal fragment (BNP) and a 76 amino acid N-terminal fragment (NT-ProBNP) during secretion or after entering the blood. The cardiomyocytes are pulled and overloaded by vascular transmural pressure to participate in the synthesis and release of BNP. BNP is the most prominent natriuretic peptide in the ventricles, with a biological half-life of about 20 minutes. The metabolic pathway of BNP in blood is not affected by the kidneys. Therefore, BNP is a more sensitive and specific index for evaluating ventricular overload compared with other natriuretic peptides and precursors thereof, can be used for diagnosing and treating heart failure (CHF), is an objective index for diagnosing heart failure, and is beneficial to diagnosis, identification, risk stratification and prognosis evaluation of heart failure. With the popularization of BNP application, the clinical application of BNP has wider prospect.
However, the stability of the calibration product in the existing kit for measuring the type B natriuretic peptide is poor, thereby causing deviation in sample detection.
Disclosure of Invention
In order to solve the technical problem that the sample detection has deviation due to poor stability of a calibrator in the existing kit for measuring the B-type natriuretic peptide, the embodiment of the invention provides a buffer solution, a calibrator, a kit, a preparation method and application.
The embodiment of the invention is realized by the following technical scheme:
in a first aspect, embodiments of the present invention provide a buffer solution comprising a papain inhibitor and aprotinin.
Further, the buffer solution containing the papain inhibitor and the aprotinin is Tris-HCl buffer solution containing the papain inhibitor and the aprotinin.
Further, the Tris-HCl buffer solution containing the papain inhibitor and the aprotinin comprises the following components:
papain inhibitor at a concentration of 25ug/mL-150ug/mL; and
aprotinin, at a concentration of 0.5ug/mL-2ug/mL.
In a second aspect, embodiments of the present invention provide a calibrator, which is a mixture of the buffer and BNP antigen.
In a third aspect, embodiments of the present invention provide the use of a calibrator for determining type B natriuretic peptides.
In a fourth aspect, embodiments of the present invention provide a kit for determining natriuretic peptide type B, comprising: a calibrator according to any one of claims 1 to 3; the calibrator also contains bovine serum albumin, PC-950 and Tween-20.
Further the kit further comprises:
analyzing the buffer;
an enzyme working solution; and
the magnetic bead coated with goat monoclonal antibody is marked with biotin.
Further, the goat monoclonal antibody-coated magnetic beads are Biotin-B type natriuretic peptide monoclonal antibody-coated magnetic beads.
Further, the enzyme working solution is a mixed solution of a buffer solution containing protein and an enzyme-labeled antibody.
In a fifth aspect, an embodiment of the present invention provides a method for preparing a buffer solution, including:
the bovine serum albumin, PC-950, tween-20, papain inhibitor and aprotinin are added into Tris-HCl buffer solution to prepare the kit.
Compared with the prior art, the embodiment of the invention has the following advantages and beneficial effects:
according to the buffer solution, the calibrator, the kit, the preparation method and the application of the embodiment of the invention, the papain inhibitor and the aprotinin aldehyde peptide are added into the buffer solution, so that degradation of BNP antigen can be inhibited during use, stability of the calibrator is improved, and accuracy of a sample detected by the kit in clinical application is improved to a certain extent.
Detailed Description
The present invention will be described in further detail with reference to the following examples, for the purpose of making the objects, technical solutions and advantages of the present invention more apparent, and the description thereof is merely illustrative of the present invention and not intended to be limiting.
In the following description, numerous specific details are set forth in order to provide a thorough understanding of the present invention. However, it will be apparent to one of ordinary skill in the art that: no such specific details are necessary to practice the invention.
Examples
The method aims at solving the technical problem that the sample detection has deviation due to poor stability of a calibrator in the existing kit for measuring the B-type natriuretic peptide; in a first aspect, embodiments of the present invention provide a buffer solution comprising a papain inhibitor and aprotinin; the papain inhibitor and the aprotinin are added into the buffer solution, so that degradation of BNP antigen can be inhibited and inhibited during use, stability of a calibrator is improved, and accuracy of a detection sample of the kit in clinical application is improved to a certain extent.
Further, the buffer solution containing the papain inhibitor and the aprotinin is Tris-HCl buffer solution containing the papain inhibitor and the aprotinin.
Further, the Tris-HCl buffer solution containing the papain inhibitor and the aprotinin comprises the following components:
papain inhibitor at a concentration of 25ug/mL-150ug/mL; and
aprotinin, at a concentration of 0.5ug/mL-2ug/mL.
In a second aspect, embodiments of the present invention provide a calibrator, which is a mixture of the buffer and BNP antigen.
In a third aspect, embodiments of the present invention provide the use of a calibrator for determining type B natriuretic peptides.
In a fourth aspect, embodiments of the present invention provide a kit for determining natriuretic peptide type B, comprising: a calibrator according to any one of claims 1 to 3; the calibrator also contains bovine serum albumin, PC-950 and Tween-20.
Further the kit further comprises:
analyzing the buffer;
an enzyme working solution; and
the magnetic bead coated with goat monoclonal antibody is marked with biotin.
Further, the goat monoclonal antibody-coated magnetic beads are Biotin-B type natriuretic peptide monoclonal antibody-coated magnetic beads.
Further, the enzyme working solution is a mixed solution of a buffer solution containing protein and an enzyme-labeled antibody.
In a fifth aspect, an embodiment of the present invention provides a method for preparing a buffer solution, including:
the bovine serum albumin, PC-950, tween-20, papain inhibitor and aprotinin are added into Tris-HCl buffer solution to prepare the kit.
Example 1
A kit for determining B-type natriuretic peptide comprises a calibrator, magnetic beads coated with goat monoclonal antibody, an analysis buffer solution and an enzyme working solution, wherein biotin is marked on the magnetic beads coated with goat monoclonal antibody.
The preparation method of the buffer solution containing 25ug/mL Antipain (papain inhibitor) and 0.5ug/mL aprotinin for preparing the calibrator comprises the following steps:
A. clean containers were prepared, 1.21g Tris, 9.0g NaCl were weighed using a laboratory balance, and about 900mL purified water was added for dissolution.
B. And (C) adding a proper amount of hydrochloric acid into the solution obtained in the step A, and adjusting the pH value to 7.35-7.45 by using 0.7mL of hydrochloric acid.
C. To the solution obtained in step B were added 10.0g BSA, 25.0mg anti-pain, 0.5mg aprotinin, 1.0mLPC-950 and 0.5 mLTwen-20.
D. The solution obtained in C was fixed to 1L with purified water to prepare a calibrator buffer containing 25ug/mL of anti-pain and 0.5ug/mL of aprotinin.
Example 2
A kit for determining B-type natriuretic peptide comprises a calibrator, magnetic beads coated with goat monoclonal antibody, an analysis buffer solution and an enzyme working solution, wherein biotin is marked on the magnetic beads coated with goat monoclonal antibody.
The preparation method of the buffer solution containing 50ug/mL Antipain and 1.0ug/mL aprotinin for preparing the calibrator comprises the following steps:
A. clean containers were prepared, 1.21g Tris, 9.0g NaCl were weighed using a laboratory balance, and about 900mL purified water was added for dissolution.
B. And (C) adding a proper amount of hydrochloric acid into the solution obtained in the step A, and adjusting the pH value to 7.35-7.45 by using 0.7mL of hydrochloric acid.
C. To the solution obtained in step B were added 10.0g BSA, 50.0mg anti-pain, 1.0mg aprotinin, 1.0mLPC-950 and 0.5 mLTwen-20.
D. The solution obtained in C was fixed to 1L with purified water to prepare 50ug/mL of anti-pain and 1.0ug/mL of aprotinin calibrator buffer.
Example 3
A kit for determining B-type natriuretic peptide comprises a calibrator, magnetic beads coated with goat monoclonal antibody, an analysis buffer solution and an enzyme working solution, wherein biotin is marked on the magnetic beads coated with goat monoclonal antibody.
The preparation method of the buffer solution containing 150ug/mL Antipain and 2.0ug/mL aprotinin for preparing the calibrator comprises the following steps:
A. clean containers were prepared, 1.21g Tris, 9.0g NaCl were weighed using a laboratory balance, and about 900mL purified water was added for dissolution.
B. And (C) adding a proper amount of hydrochloric acid into the solution obtained in the step A, and adjusting the pH value to 7.35-7.45 by using 0.7mL of hydrochloric acid.
C. To the solution obtained in step B were added 10.0g BSA, 150.0mg anti-pain, 2.0mg aprotinin, 1.0mLPC-950 and 0.5 mLTwen-20.
D. The solution obtained in C was fixed to 1L with purified water to prepare an anti-pain and aprotinin calibrator buffer at a concentration of 150ug/mL and 2.0 ug/mL.
Comparative experiments
Experiment one
And under the same condition, carrying out a calibrator thermal stability and sample detection comparison experiment without adding protease inhibitor buffer, anti-protease aldehyde peptide buffer containing anti-pain and APMSF and aprotinin B buffer.
Experimental materials: BNCHS, 0.2mol/L PBS (pH 7.4) Buffer, 1mmol/L Tris Buffer, goat anti-human BNP-specific monoclonal antibody, buffer containing 1% BSA, ALP-labeled BNP monoclonal antibody, naked magnetic beads, BNP calibrator Cal-1, cal-6 (concentration of Cal-1 to Cal-6 is 0,25,100,500,2500,5000) prepared with no protease inhibitor Buffer, aprotinin-containing aprotinin-aldehyde peptide Buffer and APMSF-and aprotinin B-containing Buffer, respectively, sample S1-S40, substrate solution, washing solution, beckmann full-automatic luminescence assay Access2.
The procedure of example 1 was followed, and the above-mentioned BNP calibrator prepared with protease inhibitor-free Buffer, anti-pain containing aprotinin aldehyde peptide Buffer and APMSF-and aprotinin B-containing Buffer, respectively, was divided into 2 parts, one part was placed at 4℃and one part was placed at 37℃with biotin antibody-coated magnetic beads, and enzyme working solution and Buffer containing 1% BSA were combined to form a kit, and after 6 days, cal-1 to Cal-6 of the calibrator at BNP4℃and 37℃were measured, and the measurement curves of the different calibrator were observed, and samples S1-S40 were measured and compared with Beckmann values. The experimental results are shown in tables 1 and 2 below.
TABLE 1
TABLE 2
Conclusion of experiment: buffer solution without protease inhibitor, calibrator containing APMSF and aprotinin B buffer, and calibrating system to detect high sample after 6 days of thermal stability; and a calibrator containing anti-pain and aprotinin is adopted, and after 6 days of thermal stability, the calibration system detection sample is well compared with Beckmann measurement values. And the stability of a calibrator containing anti-pain and aprotinin buffer is improved, and the detection accuracy of a sample is improved.
Experiment two buffer calibrator heat stability comparison experiments containing APMSF and aprotinin B at different concentrations
APMSF and aprotinin B concentrations were adjusted as in example 1, experimental example 2 and experimental example 3, and differences between batches were observed.
Experimental materials: BNCHS, 0.2mol/L PBS (PH 7.4) Buffer solution, 1mmol/L Tris Buffer solution, sheep anti-human BNP specific monoclonal antibody, buffer solution Buffer containing 1% BSA, ALP marked BNP monoclonal antibody, naked magnetic beads, BNP calibrator Cal-1 prepared by adding APMSF and aprotinin B with different concentrations respectively by using Buffer solution, cal-6 (the concentration of Cal-1 to Cal-6 is 0,25,100,500,2500,5000), samples S1-S40, substrate solution, cleaning solution and Beckmann full-automatic chemiluminescence determinator Access2.
Experimental methods reference experiment one. The experimental results are shown in table 3 below.
TABLE 3 Table 3
Conclusion of experiment:
the same calibrator diluent is added with the same protease inhibitor, but the concentration is different, and the effect of the kit prepared according to the same labeling method is not obvious, and the concentration is irrelevant to the stability of the kit.
The anti-pain and aprotinin with different concentrations are added into the diluent of the experiment three calibrator, and the thermal stability and the long-term stability of the calibrator are compared
And (3) adding anti-pain and aprotinin to the calibrator diluent according to the methods of the first experiment, the second experiment and the third experiment to regulate the concentration of the aprotinin and observe the batch-to-batch difference.
Experimental materials: BNCHS, 0.2mol/L PBS (PH 7.4) Buffer solution, 1mmol/L Tris Buffer solution, sheep anti-human BNP specific monoclonal antibody, buffer solution Buffer containing 1% BSA, ALP marked BNP monoclonal antibody, naked magnetic beads, BNP calibrator Cal-1 prepared by adding different concentrations of anti-pain and aprotinin to the Buffer solution respectively, cal-6 (the concentration of Cal-1 to Cal-6 is 0,25,100,500,2500,5000), samples S1-S40, substrate solution, cleaning solution and Beckmann full-automatic chemiluminescence determinator Access2. Experimental methods referring to experiment one, the experimental results are shown in tables 4 and 5.
TABLE 4 Table 4
Conclusion of experiment: the calibrator is also added with anti-pain and aprotinin with different concentrations in the calibrator diluent, and the calibrator has good thermal stability when 50ug/mL anti-pain and 1.0ug/mL aprotinin are added, and has poor stability when the concentration is lower and the effect is not great when the concentration is higher than 50ug/mL anti-pain and 1.0ug/mL aprotinin.
TABLE 5
Conclusion of experiment: the long-term stability of the calibrator is good when 50ug/mL of anti-pain and 1.0ug/mL of aprotinin are added into the calibrator diluent.
From four experiments, it can be derived that: the BNP assay kit is shown to have effectively improved stability when anti-pain and aprotinin are added into the calibrator diluent. When the stability of the calibrator is adjusted to 50ug/mL of anti-pain and 1.0ug/mL of aprotinin, the calibrator has good stability, the stability is slightly poor when the calibrator is too low, and resources are wasted when the calibrator is too high.
The foregoing description of the embodiments has been provided for the purpose of illustrating the general principles of the invention, and is not meant to limit the scope of the invention, but to limit the invention to the particular embodiments, and any modifications, equivalents, improvements, etc. that fall within the spirit and principles of the invention are intended to be included within the scope of the invention.
Claims (7)
1. A calibrator comprising a mixture of a buffer and a BNP antigen;
the buffer solution is a buffer solution containing a papain inhibitor and aprotinin;
the buffer solution containing the papain inhibitor and the aprotinin is Tris-HCl buffer solution containing the papain inhibitor and the aprotinin;
the Tris-HCl buffer solution containing the papain inhibitor and the aprotinin comprises the following components:
papain inhibitor at a concentration of 25ug/mL-150ug/mL; and
aprotinin, at a concentration of 0.5ug/mL-2ug/mL.
2. Use of the buffer of claim 1 or the calibrator for determining type B natriuretic peptide.
3. A kit for determining type B natriuretic peptide comprising: the calibrator of claim 1; the calibrator also contains bovine serum albumin, PC-950 and Tween-20.
4. A kit for determining natriuretic peptide type B according to claim 3, further comprising: analyzing the buffer;
an enzyme working solution; and
the magnetic bead coated with goat monoclonal antibody is marked with biotin.
5. The kit for determining type B natriuretic peptide according to claim 4, wherein the magnetic beads coated with goat monoclonal antibody are magnetic beads coated with Biotin-type B natriuretic peptide monoclonal antibody.
6. The kit for measuring type B natriuretic peptide according to claim 5, wherein the enzyme working solution is a mixed solution of a buffer solution containing a protein and an enzyme-labeled antibody.
7. A method of preparing the buffer of claim 1, comprising:
the bovine serum albumin, PC-950, tween-20, papain inhibitor and aprotinin are added into Tris-HCl buffer solution to prepare the kit.
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Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1133616A (en) * | 1993-10-22 | 1996-10-16 | 德克萨斯大学董事会 | A novel nuclear mitotic phosphoprotein:mitosin |
| WO2008056034A1 (en) * | 2006-11-10 | 2008-05-15 | Hytest Ltd. | Stable standards for bnp immunoassays |
| CN112876553A (en) * | 2021-01-18 | 2021-06-01 | 宁波海壹生物科技有限公司 | Stable B-type natriuretic peptide calibrator and preparation method thereof |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE69830668T3 (en) * | 1997-10-24 | 2011-07-14 | Shionogi & Co., Ltd. | PROCESS FOR INHIBITING THE DEGRADATION OF NATRIURETIC PEPTIDES AND IMPROVED METHOD FOR DETERMINING THE NATRIURETIC PEPTIDES |
| CA2430889A1 (en) * | 2002-06-19 | 2003-12-19 | Bayer Corporation | Stabilization of brain natriuretic peptide (bnp) in blood samples, methods and compositions related thereto |
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Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1133616A (en) * | 1993-10-22 | 1996-10-16 | 德克萨斯大学董事会 | A novel nuclear mitotic phosphoprotein:mitosin |
| WO2008056034A1 (en) * | 2006-11-10 | 2008-05-15 | Hytest Ltd. | Stable standards for bnp immunoassays |
| CN112876553A (en) * | 2021-01-18 | 2021-06-01 | 宁波海壹生物科技有限公司 | Stable B-type natriuretic peptide calibrator and preparation method thereof |
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