CN117024595B - Monoclonal antibody against human ST2 and use thereof - Google Patents
Monoclonal antibody against human ST2 and use thereof Download PDFInfo
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- 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
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- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
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- 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
- G01N33/6863—Cytokines, i.e. immune system proteins modifying a biological response such as cell growth proliferation or differentiation, e.g. TNF, CNF, GM-CSF, lymphotoxin, MIF or their receptors
- G01N33/6869—Interleukin
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- 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
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- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
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- G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
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- G01N2333/715—Assays involving receptors, cell surface antigens or cell surface determinants for cytokines; for lymphokines; for interferons
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- G01N2800/00—Detection or diagnosis of diseases
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Abstract
The invention belongs to the technical field of biology, and relates to an anti-human ST2 monoclonal antibody and application thereof, wherein the anti-human ST2 monoclonal antibody comprises a capture antibody and a detection antibody, the capture antibody comprises an amino acid sequence shown as SEQ ID NO.1 and an amino acid sequence shown as SEQ ID NO.2, and the detection antibody comprises an amino acid sequence shown as SEQ ID NO.17 and an amino acid sequence shown as SEQ ID NO. 18. The invention discloses a monoclonal antibody with high affinity and specificity against human ST2, in particular a monoclonal antibody which can form a double-antibody sandwich detection function.
Description
Technical Field
The invention relates to the technical field of biological medicine, in particular to an anti-human ST2 monoclonal antibody and application thereof.
Background
Human soluble growth stimulatory expressed gene 2 protein (Growth Stimulation Expressed Gene, st 2), one of the members of the IL-1 (interleukin 1) receptor family. St2 is found to be expressed by cardiac fibroblasts and cardiomyocytes, a cardiomyopathy protein induced by biomechanical stress, and its gene is expressed in mast cells, activated helper T cells 2 (Th 2), macrophages and cardiomyocytes. sST2 (soluble ST 2) in human blood can competitively bind to IL-33, so that cardiac muscle is affected, cardiac structure and function are affected, and the disease development rate is increased. Therefore, when heart failure occurs, the level of sST2 is significantly increased, and thus the damage effect on the heart is increased, and sST2 plays an important role in diagnosis, treatment and risk prediction of heart failure patients as a new generation heart failure marker.
The immunoassay technology based on antigen-antibody specific recognition and combination plays an important role in the field of accurate and rapid detection of ST2, such as common ELISA, fluorescent immunochromatography test paper, latex immune turbidimetry and other methods. Antibody species used in the immunoassay field include polyclonal antibodies, monoclonal antibodies, antibody fragments prepared based on genetic engineering techniques, single domain heavy chain antibodies, and the like. Among them, monoclonal antibodies are highly homogeneous antibodies raised against only a specific epitope by a single B cell clone. Monoclonal antibodies are typically prepared by hybridoma cell technology, e.g., by fusing murine myeloma cells with antigen-immunized, germ-line mouse B cells, known as hybridoma cells, which have the characteristics of unlimited in vitro propagation and synthesis and secretion of specific antibodies.
How to obtain the monoclonal antibody of high affinity and specificity anti-human ST2, in particular to a monoclonal antibody which can form a double-antibody sandwich detection function, has a crucial effect on the high-sensitivity and accurate detection of ST2, and is also a key point for limiting the performance of an immunoassay method of ST 2.
Disclosure of Invention
The invention provides an anti-human ST2 monoclonal antibody and application thereof, so as to obtain a high-affinity and specific anti-human ST2 monoclonal antibody, in particular to a monoclonal antibody with a double-antibody sandwich detection function.
In one aspect, the invention provides a monoclonal antibody against human ST2, comprising a capture antibody (abbreviated as C11 in the present invention) and a detection antibody (abbreviated as D12 in the present invention);
the capture antibody comprises the amino acid sequence: EVLLQQSGPELVKPGASVKIPCKASGYTFTDYNMDWVKQSHGKNLEWIGDIDPNNGGTIYNQKFKGKATLTVDKSSSTAYMELRSLTSEDSGVYYCARFDAYFSYWYFDVWGAGTTVTVSS (SEQ ID NO. 1) and amino acid sequence: DIVLTQSPASLAVSLGQRATISYRASKSVSTSGYSYMHWNQQKPGQPPRLLIYLVSNLESGVPARFSGSGSGTDFTLNIHPVEEEDAATYYCQHIRELNTFGGGTKLEIK (SEQ ID NO. 2);
the detection antibody comprises an amino acid sequence: QVTLKESGPGILQPSQTLSLTCSFSGFSLSTSGMGVGWIRQPSGKGLEWLAHIWWDDVKQYNPALKSRLTISKDTSSSQVFLKIASVDTADIATYYCARLGGNWDYFDYWGQGTTLTVSS (SEQ ID NO. 15) and DIVLTQSPASLVVSLGQRATISCRASESVDSCGVSFMKWLQQKPGQPPKLLIYVASKVESGVPARFGGSGSGTDFSLNIHPVEEDDFAVYFCQQSRKVPWTFGGGTKLEIK (SEQ ID NO. 16).
The monoclonal antibody against human ST2, wherein the nucleotide sequence of the amino acid sequence shown as SEQ ID NO.1 is: gaggtcctgctgcaacagtctggacctgagctggtgaagcctggggcttcagtgaagataccctgcaaggcttctggatacacattcactgactacaacatggactgggtgaagcagagtcatggaaagaaccttgagtggattggagatattgatcctaacaatggtggtactatctacaatcagaagttcaagggcaaggccacattgactgttgacaagtcctccagcacagcctacatggagctccgcagcctgacatctgaggactctggagtctattactgtgcaagatttgatgcttactttagctactggtacttcgatgtctggggcgcagggaccacggtcaccgtctcctca (SEQ ID NO. 3);
the nucleotide sequence encoding the amino acid sequence shown in SEQ ID NO.2 is: gacattgtgctgacacagtctcctgcttccttagctgtatctctggggcagagggccaccatctcatacagggccagcaaaagtgtcagtacatctggctatagttatatgcactggaaccaacagaaaccaggacagccacccagactcctcatctatcttgtatccaacctagaatctggggtccctgccaggttcagtggcagtgggtctgggacagacttcaccctcaacatccatcctgtggaggaggaggatgctgcaacctattactgtcagcacattagggagcttaacacgttcggaggggggaccaagctggaaataaaa (SEQ ID NO. 4);
the nucleotide sequence encoding the amino acid sequence shown as SEQ ID NO. 15 is: caggttactctgaaagagtctggccctgggatattgcagccctcccagaccctcagtctgacttgttctttctctgggttttcactgagcacttctggtatgggtgtaggctggattcgtcagccatcagggaagggtctggagtggctggcacacatttggtgggatgatgtcaagcagtataacccagccctgaagagccgactgactatctccaaggatacctccagcagccaggtattcctcaagatcgccagtgtggacactgcagatattgccacatactactgtgctcgattaggcgggaactgggactactttgactactggggccaaggcaccactctcacagtctcctca (SEQ ID NO. 17);
the nucleotide sequence encoding the amino acid sequence shown as SEQ ID NO. 16 is: gacattgtgctcacccaatctccggcttctttggttgtgtctctagggcagagggccaccatctcctgcagagccagcgaaagtgttgacagttgtggcgttagttttatgaagtggctccaacagaaaccaggacagccacccaaactcctcatctatgttgcatccaaagtagaatctggggtccctgccaggtttggtggcagtgggtctgggacagacttcagcctcaacatacatcctgtggaggaggatgattttgcagtttatttctgtcagcaaagtaggaaggttccttggacgttcggtggaggcaccaagctggaaatcaaa (SEQ ID NO. 18).
The monoclonal antibody against human ST2, wherein the amino acid sequences CDR1, CDR2 and CDR3 of the complementarity determining regions of the heavy chain of the capture antibody are respectively:
CDR1:GYTFTDYN(SEQ ID NO .5);
CDR2:IDPNNGGT(SEQ ID NO .6);
CDR3:ARFDAYFSYWYFDV(SEQ ID NO .7)。
the amino acid sequence CDR1 of the complementarity determining region of the light chain of the capture antibody is: KSVSTSGYSY (SEQ ID NO. 8), the amino acid sequence CDR2 of the complementarity determining region of the light chain of the capture antibody being: LVS, the amino acid sequence CDR3 of the complementarity determining region of the light chain of the capture antibody is: QHIRELNT (SEQ ID NO. 9).
The amino acid sequences CDR1, CDR2 and CDR3 of the complementarity determining regions of the heavy chain of the detection antibody are respectively:
CDR1:GFSLSTSGMG(SEQ ID NO .19);
CDR2:IWWDDVK(SEQ ID NO .20);
CDR3:ARLGGNWDYFDY(SEQ ID NO .21);
the amino acid sequence CDR1 of the complementarity determining region of the light chain of the detection antibody is: ESVDSCGVSF (SEQ ID NO. 22), the amino acid sequence CDR2 of the complementarity determining region of the light chain of said detection antibody being: VAS, the amino acid sequence CDR3 of the complementarity determining region of the light chain of the detection antibody is: QQSRKVPWT (SEQ ID NO. 23).
The monoclonal antibody against human ST2, wherein the nucleotide sequence of the amino acid sequence shown as SEQ ID NO. 5 is: ggatacacattcactgactacaac (SEQ ID NO. 10);
the nucleotide sequence encoding the amino acid sequence shown in SEQ ID NO. 6 is: attgatcctaacaatggtggtact (SEQ ID NO. 11);
the nucleotide sequence encoding the amino acid sequence shown in SEQ ID NO. 7 is: gcaagatttgatgcttactttagctactggtacttcgatgtc (SEQ ID NO. 12).
The nucleotide sequence encoding the amino acid sequence shown in SEQ ID NO. 8 is: aaaagtgtcagtacatctggctatagttat (SEQ ID NO. 13);
the nucleotide sequence encoding amino acid sequence LVS is cttgtatcc;
the nucleotide sequence encoding the amino acid sequence shown in SEQ ID NO. 9 is: cagcacattagggagcttaacacg (SEQ ID NO. 14);
the nucleotide sequence encoding the amino acid sequence shown as SEQ ID NO. 19 is: gggttttcactgagcacttctggtatgggt (SEQ ID NO. 24);
the nucleotide sequence encoding the amino acid sequence shown as SEQ ID NO. 20 is: atttggtgggatgatgtcaag (SEQ ID NO. 25);
the nucleotide sequence encoding the amino acid sequence shown as SEQ ID NO. 21 is: gctcgattaggcgggaactgggactactttgactac (SEQ ID NO. 26);
the nucleotide sequence encoding the amino acid sequence shown as SEQ ID NO. 22 is: gaaagtgttgacagttgtggcgttagtttt (SEQ ID NO. 27)
The nucleotide sequence encoding the amino acid sequence VAS is gttgcatcc;
the nucleotide sequence encoding the amino acid sequence shown as SEQ ID NO. 23 is: cagcaaagtaggaaggttccttggacg (SEQ ID NO. 28).
In another aspect, the invention provides an application of the monoclonal antibody against human ST2, wherein the monoclonal antibody against human ST2 is used for detecting the ST2 content in a sample in a pairing mode by adopting a double-antibody sandwich method.
The application of the monoclonal antibody against the human ST2, wherein the method of the double antibody sandwich comprises an enzyme-linked immunoassay method and an immunochromatography method.
The beneficial effects are that:
the monoclonal antibody against human ST2 provided by the invention comprises a capture antibody and a detection antibody, and experimental results show that both the capture antibody and the detection antibody have high affinity and specificity detection activity on human ST2 antigen, and the monoclonal antibody against human ST2 can be used for immunological analysis of ST2 in a double-antibody sandwich mode, and has important significance for high-sensitivity and accurate detection of ST2, including ELISA detection, immunochromatography and other immunological analysis detection types based on antigen-antibody specific reaction.
Drawings
FIG. 1 is a schematic diagram showing the results of double antibody sandwich ELISA detection of ST2 antigen and other proteins.
Detailed Description
In order that the invention may be readily understood, a more complete description of the invention will be rendered by reference to the appended drawings. Several embodiments of the invention are presented in the figures. This invention may, however, be embodied in many different forms and should not be construed as limited to the embodiments set forth herein. Rather, these embodiments are provided so that this disclosure will be thorough and complete.
EXAMPLE 1 preparation of human ST2 monoclonal antibodies
1) Animal immunization:
human ST2 antigen is taken as immunogen, the immunogen is mixed with Freund's adjuvant in equal volume, vortex oscillation is carried out until the immunogen is completely emulsified, and the immunization is carried out by adopting a BaLB/C mouse abdominal and back subcutaneous multipoint injection mode. Primary immunization was performed with freund's complete adjuvant at an immunogen dose of 100 μg/dose; the immunization was then followed with Freund's incomplete adjuvant and the immunogen dose was successively reduced, 1 immunization every 4 weeks, for a total of 3 immunizations. Two weeks after the third immunization, tail blood of the mice is taken, the serum antibody titer in the tail blood is measured by an indirect ELISA method, and the mice with the highest titers are directly boosted by using immunogen three days before fusion, wherein the immune dose is 40 micrograms/mouse.
2) Preparation and screening of hybridoma cells
Selected immunized mice were sacrificed by pulling the neck, spleens were removed from the ultra clean bench and ground, mouse myeloma cells SP2/0 were mixed with spleen cells in a ratio of 1:10, 50% PEG pre-warmed in advance was added for cell fusion, and the mixture was added dropwise to a 96-well cell culture plate with feeder cells. Observing the cell state through a microscope after fusion, performing semi-quantitative liquid exchange on the 5 th day after fusion, and continuously culturing until the seventh day, and then exchanging the whole liquid.
Cell fusion is carried out for about 7-10 days, cell supernatant in a cell culture plate is sucked, the secretion of antibodies in the cell supernatant is measured by adopting an indirect ELISA method, positive cell plate holes are screened, and subcloning is carried out by adopting a limiting dilution method. The ST2 protein is coated, a blank control hole is PBS, a negative control is a culture medium, and a positive control is serum of eyeball blood of a immunized mouse. When the positive rate of the selected monoclonal cells in the 96-hole cell culture plate reaches 100%, the selected monoclonal cells are judged to be positive monoclonal, and the selected monoclonal cells are frozen and expanded in time.
3) Preparation and purification of monoclonal antibody ascites
Taking about 8-week-old Balb/c mice, injecting liquid paraffin one week in advance for pre-stimulation, and promoting secretion and aggregation of nutrient substances in abdominal cavities of the mice. The hybridoma cell lines obtained were expanded to the desired number, centrifuged, carefully washed, resuspended in sterile 75% physiological saline and injected into the abdomen of mice by intraperitoneal injection. And collecting ascites after the abdomen of the mice is obviously enlarged for about one week, centrifuging for 10min at 10000r/min, and collecting supernatant to obtain monoclonal antibody ascites.
And purifying the collected ascites by using a Protein G affinity chromatography purification column. Before loading, ascites is filtered by a microporous membrane to be used as a loading liquid, and a binding buffer solution (0.15M NaCl,20mM Na) 2 HPO 4 pH 7.4), loading the filtered ascites to a chromatographic column, eluting with an elution buffer (0.1M citric acid, pH 2.5-3.0) after equilibration, and collecting the eluate rich in antibodies. The eluate is acidic, and the pH should be immediately adjusted to neutral using a neutralization buffer (1M Tris-HCl, pH 9.0) to prevent antibody inactivation, followed by identification by SDS-PAGE electrophoresis to obtain the capture antibody C11 and the detection antibody D12.
4) Determination of heavy and light chain variable regions of monoclonal antibody secreted by hybridoma cells
The hybridoma cell line capable of stably secreting sST2 monoclonal antibody is cultured to 1×10 6 cell/mL, discard supernatant, add 1mL Trizol reagent, gently shake, add 200. Mu.L chloroform, shake upside down for 30s, place on ice for 10min; centrifuging at 4deg.C for 15min at 12000g, transferring the supernatant to a new enzyme-free centrifuge tube, adding isopropanol of equal volume, and standing on ice for 10min; centrifuging at 4 ℃ for 10min with 12000g, discarding supernatant, adding 1mL of 75% ethanol, centrifuging at 4 ℃ for 5min with 7500g, drying in a super clean bench under low-speed ventilation for 5min, adding 30-50 mu L of enzyme-free sterile water, and mixing well to dissolve RNA. Reverse transcription was performed using 1. Mu.g total RNA as template and following the instructions of Hifair III 1st Strand cDNA Synthesis Kit kit. Designing upstream and downstream primers of a heavy chain variable region of the monoclonal antibody respectively, and amplifying cDNA obtained by reverse transcription, wherein the reaction parameters are as follows: 94℃for 5min,94℃for 10s,60℃for 20s,72℃for 30s, 25 cycles, and then 72℃for 5min. The obtained amplification product was identified by 1% agarose gel, and the sequence of the obtained product was determined.
5) Affinity constant determination
The affinity constant of the obtained anti-human ST2 monoclonal antibody is determined by adopting a biological film interference technology, and the specific orientation is as follows: fixing human ST2 recombinant protein with His histidine tag protein by adopting a capture HIS chip, then respectively adding C11 and D12 monoclonal antibodies with different concentrations diluted by PBS, analyzing interaction force between organisms, and displaying K of C11 and D12 by detection results D The values are 0.5X10 respectively -10 M and 0.2X10 g -10 M, all showed higher affinity.
EXAMPLE 2 double antibody sandwich ELISA assay for ST2 antigen
Respectively labeling monoclonal antibodies C11 and D12 by HRP enzyme, pairing the C11 monoclonal antibody and the D12 monoclonal antibody, and detecting ST2 antigen by double-antibody sandwich ELISA, wherein the specific method comprises the following steps: coating an anti-human ST2 antibody C11 (or D12) on an ELISA plate, and incubating overnight at 4 ℃; the following day, after 3 washes with PBST (10 mM PBS, 0.05% Tween-20 (v/v)), blocking with PBS containing 3% skimmed milk powder, and incubation at 37deg.C for 1 hr; mu.L of human ST2 antigen or other protein was added, incubated at 37℃for 0.5 hours, and after washing the plate, HRP enzyme-labeled anti-human ST2 antibody D12 (or C11) was added and incubated at 37℃for 1 hour. Then the color is developed by TMB substrate and readOD value, in particular OD 450 。
Referring to fig. 1, the above experimental results show that: as the concentration of the input ST2 antigen increases, the OD value of the plate hole of the monoclonal antibody shows gradient rise, while the plate hole added with non-ST 2 antigen protein does not have binding, which indicates that the obtained monoclonal antibody has excellent binding performance and specificity on ST2 antigen.
Example 3 application of monoclonal antibody in detection of ST2 antigen by immunochromatography test strip
1) Antibody labelling
The specific method comprises the steps of taking 5 mu L of 10mg/mL carboxylated fluorescent microspheres into a 2mL centrifuge tube containing 1mL of 10 mM PB (pH 6.0, containing 0.005% SDS), adding 1 mu L of 10mg/mL EDC and 2 mu L of NHSS solutions which are freshly prepared respectively, quickly mixing, and activating for 30 min at room temperature by using a vertical mixer. After the activation, centrifuging at 12000rpm for 12min, removing the supernatant, supplementing to 0.5mL with PB (pH 8.0), performing ultrasound for 10min to fully disperse, adding 25 μg of ST2 monoclonal antibody (D12), mixing well, coupling for 2h at room temperature by a rotary mixer, adding 150 μl of 2% sodium caseinate, sealing for 1h, centrifuging at 12000rpm for 12min, removing the supernatant, supplementing to 500 μl with a complex solution, and reserving at 4 ℃.
2) Preparation of immunochromatography test strip
The labeled antibody probes were mixed with a multiplex solution (5% trehalose, 1% BSA,0.5% Tween-20,0.2% Casein Na, 20mM Tris,0.02%NaN3,pH 8.5) 1:4, diluting, spraying 40 mu L/cm on the treated bonding pad, drying by blowing at 37 ℃ for 1h, assembling and cutting with NC film CN95 (ST 2 monoclonal antibody C11 with T line of 2mg/mL and goat anti-mouse secondary antibody with C line of 2 mg/mL) and sample pad to prepare the immunochromatographic test paper.
3) Detection of ST2 antigen
ST2 antigens with different concentrations are prepared by using sample loading buffer solution, the ST2 antigens are added into loading holes of test strips one by one in a dropwise manner, after the test strips are subjected to stationary chromatography for 15 minutes, fluorescent values on C, T lines are read by using a fluorescent immunochromatography test paper detector, and the results are shown in Table 1.
TABLE 1
It can be seen from Table 1 that the anti-human ST2 monoclonal antibodies of the present invention can achieve high sensitivity and wide linear range detection of ST2 antigen.
The foregoing examples illustrate only a few embodiments of the invention and are described in detail herein without thereby limiting the scope of the invention. It should be noted that it will be apparent to those skilled in the art that several variations and modifications can be made without departing from the spirit of the invention, which are all within the scope of the invention. Accordingly, the scope of protection of the present invention is to be determined by the appended claims.
Claims (2)
1. The detection kit for the human ST2 antigen is characterized by comprising a capture antibody and a detection antibody, wherein the amino acid sequences of complementarity determining regions CDR1, CDR2 and CDR3 of a heavy chain of the capture antibody are respectively shown in SEQ ID NO. 5, SEQ ID NO. 6 and SEQ ID NO. 7, the amino acid sequence of complementarity determining region CDR1 of a light chain of the capture antibody is shown in SEQ ID NO. 8, and the amino acid sequence of complementarity determining region CDR2 of a light chain of the capture antibody is shown in SEQ ID NO. 8: LVS, the amino acid sequence of CDR3 of the light chain of the capture antibody is shown as SEQ ID NO. 9;
the amino acid sequences of complementarity determining regions CDR1, CDR2 and CDR3 of the heavy chain of the detection antibody are shown in SEQ ID NO. 19, SEQ ID NO. 20 and SEQ ID NO. 21 respectively, the amino acid sequence of complementarity determining region CDR1 of the light chain of the detection antibody is shown in SEQ ID NO. 22, and the amino acid sequence of complementarity determining region CDR2 of the light chain of the detection antibody is as follows: VAS, the amino acid sequence of CDR3 of the light chain of the detection antibody is shown in SEQ ID NO. 23.
2. The kit for detecting human ST2 antigen according to claim 1, wherein the nucleotide sequences encoding the amino acid sequences shown as SEQ ID NO. 5, SEQ ID NO. 6 and SEQ ID NO. 7 are shown as SEQ ID NO. 10, SEQ ID NO. 11 and SEQ ID NO. 12 respectively, the nucleotide sequence encoding the amino acid sequence shown as SEQ ID NO. 8 is shown as SEQ ID NO. 13, the nucleotide sequence encoding the amino acid sequence LVS is cttgtatcc, and the nucleotide sequence encoding the amino acid sequence shown as SEQ ID NO. 9 is shown as SEQ ID NO. 14;
the nucleotide sequences of the amino acid sequences shown as SEQ ID NO. 19, SEQ ID NO. 20 and SEQ ID NO. 21 are shown as SEQ ID NO. 24, SEQ ID NO. 25 and SEQ ID NO. 26 respectively;
the nucleotide sequence of the amino acid sequence shown as SEQ ID NO. 22 is shown as SEQ ID NO. 27, the nucleotide sequence of the amino acid sequence VAS is shown as gttgcatcc, and the nucleotide sequence of the amino acid sequence shown as SEQ ID NO. 23 is shown as SEQ ID NO. 28.
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Citations (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN104151416A (en) * | 2013-05-15 | 2014-11-19 | 中国科学院上海巴斯德研究所 | Anti-human sST2 monoclonal antibody and application thereof |
CN111308086A (en) * | 2020-02-21 | 2020-06-19 | 苏州旭光科星抗体生物科技有限公司 | Enzyme-linked immunoassay kit for detecting soluble ST2 content and application thereof |
CN112480254A (en) * | 2019-09-12 | 2021-03-12 | 上海麦济生物技术有限公司 | Antibody for resisting human interleukin-33 receptor and preparation method and application thereof |
CN113214395A (en) * | 2020-01-21 | 2021-08-06 | 迈威(上海)生物科技股份有限公司 | anti-ST 2 antibodies and uses thereof |
WO2022239820A1 (en) * | 2021-05-13 | 2022-11-17 | 公益財団法人神戸医療産業都市推進機構 | Anti-human pd-1 agonist antibody for treating or preventing inflammatory diseases, and pharmaceutical composition containing same |
CN116199783A (en) * | 2022-12-22 | 2023-06-02 | 山东纳睿博恩生物医药科技有限公司 | ALP monoclonal antibody and application thereof |
CN116396384A (en) * | 2023-01-17 | 2023-07-07 | 武汉爱博泰克生物科技有限公司 | Rabbit monoclonal antibody aiming at mouse adiponectin, application of rabbit monoclonal antibody and double-antibody sandwich method ELISA (enzyme-linked immunosorbent assay) kit |
Family Cites Families (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2001070817A1 (en) * | 2000-03-21 | 2001-09-27 | Medical & Biological Laboratories Co., Ltd. | Monoclonal antibody and method and kit for the immunoassay of soluble human st2 with the use of the same |
IL298075A (en) * | 2020-05-12 | 2023-01-01 | Chia Tai Tianqing Pharmaceutical Group Co Ltd | St2 antigen binding protein |
-
2023
- 2023-10-08 CN CN202311288125.4A patent/CN117024595B/en active Active
Patent Citations (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN104151416A (en) * | 2013-05-15 | 2014-11-19 | 中国科学院上海巴斯德研究所 | Anti-human sST2 monoclonal antibody and application thereof |
CN112480254A (en) * | 2019-09-12 | 2021-03-12 | 上海麦济生物技术有限公司 | Antibody for resisting human interleukin-33 receptor and preparation method and application thereof |
CN113214395A (en) * | 2020-01-21 | 2021-08-06 | 迈威(上海)生物科技股份有限公司 | anti-ST 2 antibodies and uses thereof |
CN111308086A (en) * | 2020-02-21 | 2020-06-19 | 苏州旭光科星抗体生物科技有限公司 | Enzyme-linked immunoassay kit for detecting soluble ST2 content and application thereof |
WO2022239820A1 (en) * | 2021-05-13 | 2022-11-17 | 公益財団法人神戸医療産業都市推進機構 | Anti-human pd-1 agonist antibody for treating or preventing inflammatory diseases, and pharmaceutical composition containing same |
CN116199783A (en) * | 2022-12-22 | 2023-06-02 | 山东纳睿博恩生物医药科技有限公司 | ALP monoclonal antibody and application thereof |
CN116396384A (en) * | 2023-01-17 | 2023-07-07 | 武汉爱博泰克生物科技有限公司 | Rabbit monoclonal antibody aiming at mouse adiponectin, application of rabbit monoclonal antibody and double-antibody sandwich method ELISA (enzyme-linked immunosorbent assay) kit |
Non-Patent Citations (3)
Title |
---|
Anti-ST2 monoclonal antibody inhibits eosinophil infiltration in Angiostrongylus cantonensis-infected mice;Chih-Cheng Chuang et al.;《Journal of Microbiology, Immunology and Infection》;第49卷;第91-96页 * |
immunoglobulin heavy chain variable region, partial [Mus musculus], GenBank:UNP37070.1;Kuraoka, M. et al.;《GenPept》;第1-2页 * |
人可溶性生长刺激表达基因2蛋白的真核表达及多克隆抗体的制备;汪慧;《中国优秀硕士学位论文全文数据库 医药卫生科技辑》(第2期);第E059-161页 * |
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