CN107383199B - Monoclonal antibody of S-adenosylmethionine synthetase and application thereof - Google Patents
Monoclonal antibody of S-adenosylmethionine synthetase and application thereof Download PDFInfo
- Publication number
- CN107383199B CN107383199B CN201710509182.9A CN201710509182A CN107383199B CN 107383199 B CN107383199 B CN 107383199B CN 201710509182 A CN201710509182 A CN 201710509182A CN 107383199 B CN107383199 B CN 107383199B
- Authority
- CN
- China
- Prior art keywords
- monoclonal antibody
- adenosylmethionine synthetase
- seq
- antibody
- protein
- 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.)
- Active
Links
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/40—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against enzymes
-
- 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
- G01N33/573—Immunoassay; Biospecific binding assay; Materials therefor for enzymes or isoenzymes
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- 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
- C07K2317/565—Complementarity determining region [CDR]
-
- 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
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/91—Transferases (2.)
- G01N2333/9116—Transferases (2.) transferring alkyl or aryl groups other than methyl groups (2.5)
- G01N2333/91165—Transferases (2.) transferring alkyl or aryl groups other than methyl groups (2.5) general (2.5.1)
- G01N2333/91171—Transferases (2.) transferring alkyl or aryl groups other than methyl groups (2.5) general (2.5.1) with definite EC number (2.5.1.-)
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Food Science & Technology (AREA)
- Pathology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Cell Biology (AREA)
- Biotechnology (AREA)
- General Physics & Mathematics (AREA)
- Microbiology (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
The invention discloses a monoclonal antibody of S-adenosylmethionine synthetase, wherein the heavy chain variable region sequence of the monoclonal antibody comprises the amino acid sequences of CDRs shown in SEQ ID NO.2, 4 and 6; and the light chain variable region sequence comprises the amino acid sequences of the CDRs shown in SEQ ID Nos. 9, 11 and 13. The invention takes the polypeptide of the enzyme as immunogen, immunizes mice to obtain lymphocytes, and utilizes hybridoma cell fusion technology to prepare fusion cells, thus obtaining cell strains which can generate high affinity and high specificity detection and identification of the enzyme. The invention can be used for detecting the content of S-adenosylmethionine synthetase in animals and plants; the monoclonal antibody of the invention provides a tool for targeted protein research, so that deeper research on protein expression changes and protein network maps of different plant types, different strains or different development stages is realized.
Description
Technical Field
The invention belongs to the technical field of monoclonal antibody biology, and particularly relates to a monoclonal antibody of S-adenosylmethionine synthetase and application thereof.
Background
S-adenosylmethionine (SAM), known under the name S-adenosyl-methionine, is an important metabolic intermediate in animals, plants and the like, and is also an important physiologically active substance in human bodies, and participates in various biochemical reactions (Jingpei, adenosylmethionine, chemistry of life, 1995,5:49), such as in vivo transmethylation, transamination of propyl and transsulfuration (LUS C, Regulation of pathological glutaminic synthesis Sem Liv Dis,1998,18: 331-. The prior art has mostly studied SAM preparation methods.
SAM is synthesized by enzymatic synthesis of substrates L-methionine and ATP through S-adenosylmethionine synthetase, therefore, S-adenosylmethionine synthetase is a key enzyme for synthesizing SAM, and detection of the content of S-adenosylmethionine synthetase in animals and plants can reflect factors influencing SAM synthesis of animals and plants and can also be used for analytical research on detection of SAM contained in different animals and plants.
Currently, there is no targeting antibody specifically directed to S-adenosylmethionine synthetase on the market, and therefore, there is no effective antibody tool for the research field on the proteomics level, and the antibody tool is used for the research of the expression capability level of the enzyme in different plant types, different strains or different development stages.
Disclosure of Invention
The invention provides a monoclonal antibody of S-adenosylmethionine synthetase and application thereof, aiming at solving the defects in the prior art, and the invention realizes deeper research on protein expression change and protein network maps of different plant types, different strains or different development periods by providing a tool for targeted protein research.
The technical scheme of the invention is as follows:
the invention synthesizes S-adenosylmethionine synthetase polypeptide, namely four groups of 'FTKCPEEIGA' ″ TDETPELMPL '″ QVTVEYYNDK' and 'VLISTQHDET', which are used as immunogen respectively, immunizes a mouse to obtain lymphocytes, prepares fusion cells by utilizing hybridoma cell fusion technology, obtains a cell strain capable of producing monoclonal antibodies with high affinity and high specificity by an immunoblotting method, a limited dilution method and an ELISA method, and determines the most effective antibodies by verification of immunoenzyme coupling, protein imprinting, co-immunoprecipitation, mass spectrometry, antibody chip detection and the like.
A monoclonal antibody of S-adenosylmethionine synthetase, the heavy chain variable region sequence of which comprises the amino acid sequence of CDR1 shown in SEQ ID No.2, the amino acid sequence of CDR2 shown in SEQ ID No.4 and the amino acid sequence of CDR3 shown in SEQ ID No. 6; and the light chain variable region sequence comprises the amino acid sequence of CDR1 shown in SEQ ID NO.9, the amino acid sequence of CDR2 shown in SEQ ID NO.11 and the amino acid sequence of CDR3 shown in SEQ ID NO. 13.
Preferably, the framework regions of said heavy chain variable region sequence comprise in sequence the amino acid sequences shown in SEQ ID nos. 1, 3, 5 and 7, and the framework regions of said light chain variable region sequence comprise in sequence the amino acid sequences shown in SEQ ID nos. 8, 10, 12 and 14.
The invention also discloses the application of the monoclonal antibody of the S-adenosylmethionine synthetase in detecting the S-adenosylmethionine synthetase.
Preferably, the monoclonal antibody against S-adenosylmethionine synthetase is used for detecting the content of S-adenosylmethionine synthetase in animals and plants.
Compared with the prior art, the invention has the following beneficial effects:
the monoclonal antibody of S-adenosylmethionine synthetase has high affinity and high specificity to S-adenosylmethionine synthetase, can be widely used for detecting the S-adenosylmethionine synthetase, and particularly can be used for detecting the content of the S-adenosylmethionine synthetase in animals and plants; meanwhile, the enzyme content directly reflects the expression level of S-adenosylmethionine in a body, the protein mainly carries out biochemical reaction in liver and is widely applied to treatment of liver diseases such as alcoholic liver disease, drug-induced liver damage and the like, and the antibody can be used as a very effective detection means to regularly observe the cure condition of related liver disease patients. In addition, in the field of proteomics research, the monoclonal antibody of the invention provides a tool for targeted protein research, so that deeper research on protein expression changes and protein network maps of different plant types, different strains or different development stages is realized.
Drawings
FIG. 1 is a schematic diagram showing the result of WB validation of endogenous protein imprinting of cherry whole protein lysate and clone No. 2B7 anti-SAM antibody;
FIG. 2 is a schematic diagram showing the detection results of an antibody chip of cherry whole protein lysate, clone No. 2B7 anti-SAM antibody and control antibody;
FIG. 3 is a standard curve prepared by ELISA reaction of clone No. 2B7 anti-SAM antibody of the present invention with S-adenosylmethionine synthetase of different concentrations.
Detailed Description
The invention will be further illustrated with reference to the following specific examples. It should be understood that these examples are only for illustrating the present invention and are not intended to limit the scope of the present invention. In practice, the invention will be understood to cover all modifications and variations of this invention provided they come within the scope of the appended claims.
The present invention is not particularly limited, and the technical means used in the following examples are conventional technical means known to those skilled in the art, and the raw materials and reagents used are commercially available products.
EXAMPLE 1 preparation of hybridoma cell which is a monoclonal antibody against S-adenosylmethionine synthetase and preparation and purification of monoclonal antibody against S-adenosylmethionine synthetase
1.1 preparation of antigens
Four sets of S-adenosylmethionine synthetase polypeptides 'FTKCPEEIGA' ', TDETPELMPL' ', QVTVEYYNDK' and 'VLISTQHDET' were synthesized and used as immunogens, respectively, which were also coupled to VLPs and to immunogenicity enhancing factors of the conventional KLH system.
1.2 immunization of mice
Each group of antigens will be used to immunize 6 Balb/c mice (8-12 weeks old) and their serum titers monitored to determine the optimal number of immunizations. Each 6 immunogen polypeptides were mixed into one group. The optimized adjuvant and immunization method can produce high affinity antibodies (IgG subtype) against most antigenic polypeptides. After the primary immunization, 3 to 4 times of reinforcement is carried out, and after the reinforcement, the serum of the mouse is taken to detect the titer (the recombinant protein of the S-adenosylmethionine synthetase is used as an antigen coating). Mice that are eligible for titer will be bumped once and used for fusion, and ineligible mice will continue to be boosted one to two times until the titer is highest and fused.
1.3 serum detection and screening
The mice were immunized by orbital bleeding and serum titers were measured by ELISA (recombinant protein of S-adenosylmethionine synthetase as antigen coating). The serum titer needs to be more than 10K, otherwise the boosting is continued.
1.4 fusion and screening
Lymph nodes from whole spleens and 1/2 were taken and fused with myeloma SP2/0 cell line. The process is optimized PEG fusion. The fused cells were plated on 4 384-well plates (cells 102 to 104 per well) and cultured. Supernatants from all wells were collected, screened for the polypeptide assay by ELISA, and positive wells with microscopic cells were transferred to 96-well plates for further culture. After several days of growth, supernatants from all wells were collected and assayed for reaction with soluble fragment assay by ELISA. Positive wells further tested different dilutions of soluble fragment for binding to assay for affinity sequencing. The 20 parent clones with the highest affinity for each polypeptide immunogen entered subcloning. The 60 parental clones with the highest immunogenic affinity per soluble fragment entered subcloning.
1.5 subcloning and screening
Subcloning was performed by limiting dilution and ELISA screening to obtain monoclonal hybridoma cells. Cells were plated in 96-well plates and cultured to cover the bottom of about 1/6. ELISA detects the reaction of the supernatant of each hole to the soluble fragment detection antigen and the corresponding polypeptide detection antigen, and two holes with high OD values and good cell states are selected to enter the next round of subcloning. The above procedure was repeated until the positive rate of cell lines in the wells was 100%. At this point we obtained a monoclonal cell line. After the final round of subcloning, all positive cells were immediately expanded, one part was frozen for later use, and the other part was subjected to supernatant or ascites preparation.
1.6 preparation and purification of antibody supernatants
Finally, 8 monoclonal cell strains were obtained and injected ventrally into F1 mice for antibody production. The ascites fluid produced was purified with Protein A/G and used for subsequent detection.
Example 2 validation of anti-CK 18 monoclonal antibody
And (3) verifying the obtained 8 monoclonal antibody cell strains by immunoenzyme coupling, protein imprinting, co-immunoprecipitation and mass spectrometry, an antibody chip and the like to determine the most effective antibody.
2.1 Elisa (immunoenzyme-linked) pairing validation of antibodies and antigenic polypeptides
And (3) coating a 96-hole ELISA plate with the ascites antibody to be paired, incubating, washing, sealing the degreased milk overnight, washing with PBS, and storing at 4 ℃ for later use. Antigen polypeptide incubation, PBS wash, with controls. HRP-labeled detection antibody was added to the ELISA plate incubated with the aforementioned. TMB color reaction, reading by a microplate reader. The titer of 8 cell lines obtained by screening is shown in table one:
2.2 endogenous Western Blot (WB) validation of antibodies
Using cherry whole protein lysate, antibody dilution concentration 1: 1000. 1: WB verification was performed 2000 and 1: 5000. The experimental results show that anti-SAM (clone 2B7) can specifically identify the 40KD band in WB validation, which is consistent with the expected size, as shown in FIG. 1.
2.3 Co-Immunoprecipitation (IP) plus mass spectrometry validation of antibodies
1mg of cherry holoprotein was extracted, immunoprecipitation was performed using anti-SAM (clone 2B7), and 40kd size bands were excised from the IP product for mass spectrometric detection. The mass spectrum result is shown in table two, SAM is abundant in IP sample, prove this antibody to SAM recognition specificity high, and, this antibody can be applied to IP experiment.
Watch two
2.4 antibody chip assay
An anti-SAM (clone 2B7) antibody and a control antibody were spotted onto a glass plate with an NC membrane as a substrate using a chip spotting machine to form antibody spots having a diameter of 100. mu.m. Apple holoprotein is labeled by biotin, incubated on an antibody chip at the concentration of 2ug/ml, and incubated at room temperature for half an hour. The cells were gently washed three times with PBS, incubated with CY3-SA fluorescent secondary antibody, washed three times with PBS, and the chip was scanned 523nm using a GenePix fluorescent chip scanner.
The experimental result is shown in fig. 2, the Anti-SAM antibody has obvious enrichment binding effect on the target protein, the fluorescence intensity is strong, and the control antibody does not have antigen-antibody binding reaction.
EXAMPLE 3 use of the monoclonal antibody against S-adenosylmethionine synthetase of the present invention for detecting the S-adenosylmethionine synthetase content in different animals
The antibody of the invention has unique specificity to S-adenosylmethionine synthetase, and can be used as a detection antibody for specially detecting the content of S-adenosylmethionine synthetase in different animals and plants, or can be further developed into a detection kit according to conventional technical means in the field.
First, the antibody of the present invention was subjected to an ELISA test using standards of S-adenosylmethionine synthetase recombinant proteins at fixed concentrations (1mg/ml) and different concentrations to obtain corresponding OD values, and a standard curve was drawn, with the abscissa being the concentration coordinate of S-adenosylmethionine synthetase and the ordinate being the optical density value (OD value) measured by an ELISA reader, as shown in fig. 3. The standard curve is used for converting the OD value detected by the sample to be detected into the concentration of the enzyme subsequently; the recombinant protein of S-adenosylmethionine synthetase as the standard was quantified by BC protein and checked for running gel to confirm the concentration, and diluted at a ratio of 10ug/ml,5ug/ml,2.5ug/ml,1.25ug/ml, as shown in Table three.
Watch III
| Concentration of Standard substance (mg/ml) | 10 | 5 | 2.5 | 1.25 |
| OD value of standard | 2.856 | 2.154 | 1.521 | 0.857 |
Then, taking tissue fluid samples of different peaches to carry out ELISA experiments, detecting by using the same concentration (1mg/ml) of the antibody of the invention, substituting the obtained OD value into a standard curve to calculate, and obtaining the actual enzyme content and the corresponding expression level in different animals and plants, as shown in the fourth table.
Watch four
| Detecting the OD value | Conversion of enzyme concentration to mg/ml | Expression level | |
| Honey peach | 1.869 | 1.88 | In |
| Arabidopsis thaliana | 0.568 | 0.51 | Is low in |
| Zebra fish | 2.058 | 2.27 | In |
| Serum | 3.254 | 7.52 | Height of |
Example 4
Clone No. 2B7 anti-SAM antibody
Culturing hybridoma cell strain of 2B7 clone number anti-SAM antibody, extracting total RNA, and reverse transcribing mRNA into first chain cDNA; amplifying heavy chain and light chain genes through PCR, cloning the amplified genes to a sequencing vector, and performing sequencing on a plurality of positive clones to obtain a final sequence result.
The preferred embodiments of the invention disclosed above are intended to be illustrative only. The preferred embodiments are not intended to be exhaustive or to limit the invention to the precise embodiments disclosed. Obviously, many modifications and variations are possible in light of the above teaching. The embodiments were chosen and described in order to best explain the principles of the invention and the practical application, to thereby enable others skilled in the art to best utilize the invention. The invention is limited only by the claims and their full scope and equivalents.
SEQUENCE LISTING
<110> Abiramate medical technology (Shanghai) Co., Ltd
<120> monoclonal antibody of S-adenosylmethionine synthetase and application thereof
<130>2017
<160>14
<170>PatentIn version 3.5
<210>1
<211>24
<212>PRT
<213> Artificial sequence
<220>
<221>V-region
<222>(1)..(24)
<223>VHF1
<400>1
Arg Gln Leu Gln Ile Thr Gly Ser Ser Leu Val Phe Pro Ala Gln Thr
1 5 10 15
Glu AlaGlu Thr Tyr Ser Val Gly
20
<210>2
<211>8
<212>PRT
<213> Artificial sequence
<220>
<221>V-region
<222>(1)..(8)
<223>VHCDR1
<400>2
Val Phe Ile Ala Leu Thr Ala Pro
1 5
<210>3
<211>16
<212>PRT
<213> Artificial sequence
<220>
<221>V-region
<222>(1)..(16)
<223>VHF2
<400>3
Asp Asn Gln Ile Thr Met Ile Pro Met Leu Ser Leu Glu Tyr Arg Asn
1 5 10 15
<210>4
<211>7
<212>PRT
<213> Artificial sequence
<220>
<221>V-region
<222>(1)..(7)
<223>VHCDR2
<400>4
Tyr Ser Gln Leu Leu Ala Thr
1 5
<210>5
<211>19
<212>PRT
<213> Artificial sequence
<220>
<221>V-region
<222>(1)..(19)
<223>VHF3
<400>5
Thr Ala Met Met Ile Pro Ala Leu Thr Glu Ala Tyr Ser Val Gly Gly
1 5 10 15
Thr Gly Ala
<210>6
<211>4
<212>PRT
<213> Artificial sequence
<220>
<221>V-region
<222>(1)..(4)
<223>VHCDR3
<400>6
Ser Ala Val Thr
1
<210>7
<211>12
<212>PRT
<213> Artificial sequence
<220>
<221>V-region
<222>(1)..(12)
<223>VHF4
<400>7
Asn Ile Thr Pro Leu Ser Leu Leu Glu Tyr Ala Gly
1 5 10
<210>8
<211>19
<212>PRT
<213> Artificial sequence
<220>
<221>V-region
<222>(1)..(19)
<223>VLF1
<400>8
Met Ile Pro Ala Leu Glu Thr Ala Tyr Ser Ser Gly Thr Thr Leu Ala
1 5 10 15
Glu Met Val
<210>9
<211>5
<212>PRT
<213> Artificial sequence
<220>
<221>V-region
<222>(1)..(5)
<223>VLCDR1
<400>9
Ser Gly Ala Thr Ser
1 5
<210>10
<211>12
<212>PRT
<213> Artificial sequence
<220>
<221>V-region
<222>(1)..(12)
<223>VLF2
<400>10
Ser Ala Thr Tyr Ser Ser Gly Leu Ala Glu Met Gly
1 5 10
<210>11
<211>8
<212>PRT
<213> Artificial sequence
<220>
<221>V-region
<222>(1)..(8)
<223>VLCDR2
<400>11
Gly Thr Ala Asn Gln Ile Met Ala
1 5
<210>12
<211>35
<212>PRT
<213> Artificial sequence
<220>
<221>V-region
<222>(1)..(35)
<223>VLF3
<400>12
Pro Arg Phe Pro Val Ile Ile Gln Arg Leu Gly Pro Val Phe Gly Asp
1 5 10 15
Val Phe Thr Leu Thr Val Ile Met Met Gln Glu Gln Arg Leu Ser Asp
20 25 30
Tyr Glu Thr
35
<210>13
<211>10
<212>PRT
<213> Artificial sequence
<220>
<221>V-region
<222>(1)..(10)
<223>VLCDR3
<400>13
Tyr Gln Ser Thr Ile Ser Pro Glu Arg Val
1 5 10
<210>14
<211>10
<212>PRT
<213> Artificial sequence
<220>
<221>V-region
<222>(1)..(10)
<223>VLF4
<400>14
Gly Gly Ser Glu Gly Lys Val Glu Lys Thr
1 5 10
Claims (3)
1. A monoclonal antibody of S-adenosylmethionine synthetase, characterized in that the heavy chain variable region of the monoclonal antibody comprises CDR1 shown in SEQ ID NO.2, CDR2 shown in SEQ ID NO.4 and CDR3 shown in SEQ ID NO. 6; and the light chain variable region comprises CDR1 as shown in SEQ ID NO.9, CDR2 as shown in SEQ ID NO.11 and CDR3 as shown in SEQ ID NO. 13.
2. The monoclonal antibody of S-adenosylmethionine synthetase according to claim 1, wherein the framework regions of the heavy chain variable region are selected from the group consisting of SEQ ID No.1, 3, 5 and 7 in that order, and the framework regions of the light chain variable region are selected from the group consisting of SEQ ID No.8, 10, 12 and 14 in that order.
3. Use of the monoclonal antibody against S-adenosylmethionine synthetase according to claim 1 for detecting the content of S-adenosylmethionine synthetase in plants.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN2017101541427 | 2017-03-15 | ||
| CN201710154142.7A CN106831994A (en) | 2017-03-15 | 2017-03-15 | A kind of monoclonal antibody of S adenomethionine synthases and its application |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN107383199A CN107383199A (en) | 2017-11-24 |
| CN107383199B true CN107383199B (en) | 2020-03-17 |
Family
ID=59145122
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201710154142.7A Withdrawn CN106831994A (en) | 2017-03-15 | 2017-03-15 | A kind of monoclonal antibody of S adenomethionine synthases and its application |
| CN201710509182.9A Active CN107383199B (en) | 2017-03-15 | 2017-06-28 | Monoclonal antibody of S-adenosylmethionine synthetase and application thereof |
Family Applications Before (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201710154142.7A Withdrawn CN106831994A (en) | 2017-03-15 | 2017-03-15 | A kind of monoclonal antibody of S adenomethionine synthases and its application |
Country Status (1)
| Country | Link |
|---|---|
| CN (2) | CN106831994A (en) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112279917B (en) * | 2020-06-01 | 2024-01-05 | 普众发现医药科技(上海)有限公司 | Monoclonal antibody of mouse anti-cell surface glycoprotein CD138 capable of being applied to tumor cell capture |
| CN112094350B (en) * | 2020-06-01 | 2024-01-05 | 普众发现医药科技(上海)有限公司 | Monoclonal antibody of mouse anti-cell surface glycoprotein CD326 applicable to tumor cell capture |
| CN112094346B (en) * | 2020-06-01 | 2024-01-05 | 普众发现医药科技(上海)有限公司 | Monoclonal antibody of mouse anti-cell single-chain transmembrane glycoprotein CD142 capable of being applied to tumor cell capture |
| CN112094345B (en) * | 2020-06-01 | 2024-01-05 | 普众发现医药科技(上海)有限公司 | Mouse anti-immunoglobulin associated beta CD79b monoclonal antibody applicable to tumor cell capture |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5686255A (en) * | 1995-05-24 | 1997-11-11 | Deth; Richard C. | Compositions and methods for diagnosing schizophrenia |
| US6313265B1 (en) * | 1995-07-24 | 2001-11-06 | The Scripps Research Institute | Neurite outgrowth-promoting polypeptides containing fibronectin type III repeats and methods of use |
| US7045612B2 (en) * | 1998-01-16 | 2006-05-16 | Mcgill University | Human methionine synthase reductase: cloning, and methods for evaluating risk of neural tube defects, cardiovascular disease, and cancer |
| CN1307103A (en) * | 2000-01-21 | 2001-08-08 | 上海博道基因技术有限公司 | Polypeptide-S-adenosylmethionine synthetase 31 and polynucleotide for coding said polypeptide |
-
2017
- 2017-03-15 CN CN201710154142.7A patent/CN106831994A/en not_active Withdrawn
- 2017-06-28 CN CN201710509182.9A patent/CN107383199B/en active Active
Also Published As
| Publication number | Publication date |
|---|---|
| CN106831994A (en) | 2017-06-13 |
| CN107383199A (en) | 2017-11-24 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US10175249B2 (en) | Proteomic identification of antibodies | |
| CN107383199B (en) | Monoclonal antibody of S-adenosylmethionine synthetase and application thereof | |
| US20140057294A1 (en) | A hybridoma cell line 10g4 and a monoclonal antibody against the total of aflatoxin b1, b2, g1 and g2 | |
| US20220363712A1 (en) | Methods and systems for generating, validating and using monoclonal antibodies | |
| CN106866820B (en) | Monoclonal antibody for capturing tumor cells and resisting human keratin 18 and application thereof | |
| CN107266576B (en) | Monoclonal antibody of 1-aminocyclopropane-1-carboxylic oxidase and application thereof | |
| CN113150138B (en) | KPC-2 monoclonal antibody, and preparation method and application thereof | |
| WO2014152660A1 (en) | Engineered antibody scaffolds | |
| CN111647081B (en) | Recombinant mouse anti-human interleukin 19 monoclonal antibody, preparation method and application | |
| CN114591430B (en) | BSA (bovine serum albumin) monoclonal antibody, application thereof and BSA (bovine serum albumin) detection kit containing antibody | |
| WO2016019888A1 (en) | Method and system for screening for nanobodies | |
| CN111647086B (en) | Recombinant mouse anti-human creatine kinase monoclonal antibody, preparation method and application | |
| CN111303261B (en) | Monoclonal antibody for detecting grape abortion related transcription factor and application thereof | |
| EP2187216B1 (en) | Novel liver cancer marker | |
| CN113024668B (en) | DUF642 protein monoclonal antibody and application thereof | |
| CN112679607A (en) | Preparation method of troponin I E13 single-chain antibody | |
| CN107987167B (en) | Monoclonal antibody of RNA polymerase II transcription subunit 37e mediator and application thereof | |
| CN111647083B (en) | Recombinant mouse anti-human hemojulin monoclonal antibody, preparation method and application | |
| CN110950958B (en) | anti-BRCA 2 monoclonal antibody and application thereof | |
| WO2024140618A1 (en) | 1,3-β-D-GLUCAN BINDING PROTEIN, PREPARATION METHOD, AND USE | |
| CN111499751B (en) | Monoclonal antibody for detecting cabbage catalase and application thereof | |
| CN110483642B (en) | Monoclonal antibody of enoyl-acyl carrier protein reductase and application thereof | |
| CN111303291A (en) | Monoclonal antibody for detecting tobacco adenosine triphosphatase and application thereof | |
| CN111349169A (en) | Monoclonal antibody of Werner syndrome ATP-dependent helicase and application thereof | |
| CN117003866A (en) | anti-CALR mutant protein antibody, preparation method and detection kit |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant |