[go: up one dir, main page]

CN102793922A - Method for treating neoplastic disease in body of mammals - Google Patents

Method for treating neoplastic disease in body of mammals Download PDF

Info

Publication number
CN102793922A
CN102793922A CN2012102878596A CN201210287859A CN102793922A CN 102793922 A CN102793922 A CN 102793922A CN 2012102878596 A CN2012102878596 A CN 2012102878596A CN 201210287859 A CN201210287859 A CN 201210287859A CN 102793922 A CN102793922 A CN 102793922A
Authority
CN
China
Prior art keywords
ser
seq
gly
insulin
growth factor
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.)
Pending
Application number
CN2012102878596A
Other languages
Chinese (zh)
Inventor
丁兆
朱仲玉
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Sichuan Huiyu Pharmaceutical Co Ltd
Original Assignee
Sichuan Huiyu Pharmaceutical Co Ltd
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by Sichuan Huiyu Pharmaceutical Co Ltd filed Critical Sichuan Huiyu Pharmaceutical Co Ltd
Priority to CN2012102878596A priority Critical patent/CN102793922A/en
Publication of CN102793922A publication Critical patent/CN102793922A/en
Pending legal-status Critical Current

Links

Images

Landscapes

  • Peptides Or Proteins (AREA)

Abstract

本发明公开了一种治疗哺乳动物体内肿瘤疾病的方法,它包括:给药物至哺乳动物主体;所述的药物包括抗体,所述的抗体中含有SEQIDNO:1,SEQIDNO:2,SEQIDNO:3,SEQIDNO:4,SEQIDNO:5,SEQIDNO:6,SEQIDNO:7或SEQIDNO:8中记载的氨基酸序列;所述的抗体特异性地结合到胰岛素样生长因子I上,所述的抗体也可以特异性地结合到胰岛素样生长因子II上。本发明将具有特定氨基酸序列的抗体的药物作用于哺乳动物本体,抗体与胰岛素样生长因子特异性结合,阻止胰岛素样生长因子与胰岛素样生长因子受体结合,从而减少或者消除哺乳动物体内的肿瘤疾病。

The invention discloses a method for treating tumor diseases in mammals, which comprises: giving medicine to the mammal body; the medicine includes antibodies, and the antibodies contain SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, The amino acid sequence recorded in SEQIDNO: 4, SEQIDNO: 5, SEQIDNO: 6, SEQIDNO: 7 or SEQIDNO: 8; the antibody specifically binds to insulin-like growth factor I, and the antibody can also specifically Binds to insulin-like growth factor II. The invention acts on the mammal body with the drug of the antibody having a specific amino acid sequence, and the antibody specifically binds to the insulin-like growth factor, prevents the insulin-like growth factor from binding to the insulin-like growth factor receptor, thereby reducing or eliminating tumors in the mammalian body disease.

Description

A kind of method of treating tumor disease in the mammalian body
Technical field
The invention belongs to biological field, particularly, relate to a kind of method of treating tumor disease in the mammalian body.
Background technology
Cell division and cell proliferation faster can cause the incidence probability of cancer to improve.Clinical research in recent years shows that the morbidity of insulin like growth factor and multiple common cancer (like breast carcinoma, carcinoma of prostate, pulmonary carcinoma and colon cancer etc.) has direct relation.Insulin like growth factor is brought into play in mitosis and is regulated cell proliferation, differentiation and effect of apoptosis, it not only the irritation cell proenzyme also suppress apoptosis, this generation to tumor has direct influence.The effect of insulin like growth factor mediates through IGF-1.Insulin-like growth factor I and insulin-like growth factor II mediate its effect through being attached to IGF-1.
The expression of IGF-1 is higher than the normal structure of closing in multiple cancerous cell, and its propagation of mediation and transfer in the process of cancer cell-apoptosis.Insulin like growth factor is attached on the IGF-1, and activate EGFR-TK the propagation of cell is strengthened, and the signal path through comprising PI3 kinases/Akt and the existence of MAPK approach mediated cell.Stop insulin like growth factor and IGF-1 combine the required signal mediation of cell proliferation is suppressed, thereby reduce the incidence probability of perhaps eliminating cancer.
So, in the art, be necessary that development stops insulin like growth factor and the bonded method of IGF-1.
Summary of the invention
The technical problem that will solve required for the present invention provides a kind of method of treating tumor disease in the mammalian body.The drug effect of the antibody through will having the specific amino acids sequence that the application puts down in writing is in the mammal body; Can stop insulin like growth factor to combine, perhaps eliminate the intravital tumor disease of mammal thereby reduce with IGF-1.
It is following that the present invention solves the problems of the technologies described above the technical scheme that is adopted:
A kind of method of treating tumor disease in the mammalian body, it comprises: give medicine to mammal main body; Described medicine comprises antibody, contains SEQ ID NO:1 in the described antibody, SEQ ID NO:2; SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5; SEQ ID NO:6, the aminoacid sequence of putting down in writing among SEQ ID NO:7 or the SEQ ID NO:8; Be attached on the insulin-like growth factor I to described antibody specificity, can reduce or eliminate the intravital tumor disease of mammal.
Be attached on the insulin-like growth factor I to described antibody specificity, can reduce or eliminate the intravital tumor disease of mammal.
Described antibody also can be attached on the insulin-like growth factor II specifically.
Described tumor disease is solid tumor, hematologic malignancies, leukemia, colorectal cancer, optimum or malignant breast carcinomas, uterus carcinoma, hysteromyoma, ovarian cancer, carcinoma of endometrium, polycystic ovary syndrome, endometrial polyp, carcinoma of prostate, prostate hyperplasia, hypophysis cerebri cancer, adenomyosis, adenocarcinoma, meningioma, melanoma, bone tumor, multiple myeloma, central nervous system cancer, glioma or astroblast cancer.
Particularly, described tumor disease is meant that the intravital tumor cell of described mammal shifts.
Particularly, described tumor disease is meant the intravital Metastasis in Breast Cancer of described mammal.
The invention has the beneficial effects as follows: the present invention will have the drug effect of antibody of specific amino acids sequence in the mammal body; Antibody combines with specific for insulin-like growth factors; Stop insulin like growth factor to combine with IGF-1; Suppress insulin like growth factor in vivo or the ability of vivoexpression cell proliferation, thereby reduce or eliminate the intravital tumor disease of mammal.
Description of drawings
Fig. 1 has showed that AC112, AC113 and AC122 are attached to the situation of insulin-like growth factor I
Fig. 2 has showed that AC112, AC113 and AC122 are attached to the situation of insulin-like growth factor II
Fig. 3 has showed that the situation that AC122 and AC122-1 are attached to insulin-like growth factor I and insulin-like growth factor II shows
Fig. 4 has showed AC122-1 inhibition to the IGF-1 phosphorylation in the MCF-7 breast cancer cell
Fig. 5 has showed the inhibition that AC122-1 shifts the MCF-7 breast cancer cell.
The specific embodiment
Below in conjunction with specific embodiment the present invention is described in further detail, protection scope of the present invention is not limited only to following embodiment.
Embodiment 1:
At present, most of available insulin like growth factor antibody is not from the mankind, but from muroid.The inventor utilizes and comprises 10 10The monoclonal antibody to insulin like growth factor is developed in the human source Fab storehouse that individual different bacteriophages is showed.Through enzyme linked immunosorbent assay, utilize insulin-like growth factor I as target antigen, through the three-wheel screening, obtain 200 random individual phage clones.Monoclonal antibody to obviously being attached to insulin-like growth factor I checks order, and wherein 3 monoclonal antibodies have unique sequence, and they are expressed with solubility Fab in phage.One of them monoclonal antibody AC122 is in above-mentioned enzyme linked immunosorbent assay detects; Insulin-like growth factor I and insulin-like growth factor II are all demonstrated stronger binding specificity; Two other monoclonal antibody, AC112 and AC113 then only demonstrate binding specificity to insulin-like growth factor I.
The human source Fab storehouse is as the source of upsetting the whole ingredients of specific antibody chain variable region gene VL in the storehouse.When the preparation of phage is carried out in the human source Fab storehouse, at first carry out enzyme action with Nco I and Spe I, carry out agarose gel electrophoresis then, to remove all specific antibody heavy chain variable region gene VH.Gene code to the VH district of monoclonal antibody AC122 increases, and introduces random mutation, merges mutually with the genetic fragment of CHI then.Merge fragment and carry out enzyme action, then its purification from gel is come out, and be connected to the main body carrier of purification, obtain upsetting whole ingredients of specific antibody chain variable region gene VL in the storehouse through Nco I and Spe I.From upset the storehouse, obtain 2 * 10 8Individual independently monoclonal antibody, said monoclonal antibody are the variant of AC122.Through to the screening of the two-wheeled of insulin-like growth factor I conjugated beads, and carry out second through enzyme linked immunosorbent assay and obtain 200 monoclonal antibodies after taking turns screening.Monoclonal antibody to obviously being attached to insulin-like growth factor I and insulin-like growth factor II checks order; Wherein 5 monoclonal antibody AC122-1 have unique sequence, and he demonstrates very strong binding specificity to insulin-like growth factor I and insulin-like growth factor II.
Wherein, the specific antibody heavy chain variable region gene VH of AC112 comprises the aminoacid sequence of putting down in writing among the SEQ ID NO:1, and the specific antibody chain variable region gene VL of AC112 comprises the aminoacid sequence of putting down in writing among the SEQ ID NO:2;
The specific antibody heavy chain variable region gene VH of AC113 comprises the aminoacid sequence of putting down in writing among the SEQ ID NO:3, and the specific antibody chain variable region gene VL of AC113 comprises the aminoacid sequence of putting down in writing among the SEQ ID NO:4;
The specific antibody heavy chain variable region gene VH of AC122 comprises the aminoacid sequence of putting down in writing among the SEQ ID NO:5, and the specific antibody chain variable region gene VL of AC122 comprises the aminoacid sequence of putting down in writing among the SEQ ID NO:6;
The specific antibody heavy chain variable region gene VH of AC122-1 comprises the aminoacid sequence of putting down in writing among the SEQ ID NO:7, and the specific antibody chain variable region gene VL of AC122-1 comprises the aminoacid sequence of putting down in writing among the SEQ ID NO:8.
Above-mentioned 4 kinds of antibody and insulin-like growth factor I or insulin-like growth factor I and insulin-like growth factor II specificity combine; There are competitive relation in antibody and IGF-1; Thereby stop insulin like growth factor to combine, make the required signal mediation of cell proliferation be suppressed with IGF-1.
As depicted in figs. 1 and 2; Test through enzyme linked immunosorbent assay; AC112 and AC113 combine with the insulin-like growth factor I specificity; Do not combine with insulin-like growth factor II, AC122 combines with insulin-like growth factor I and insulin-like growth factor II specificity, and its binding ability is superior to AC112 and AC113.
As shown in Figure 3; Through the enzyme linked immunosorbent assay test, along with the raising of AC, the binding capacity of antibody and insulin-like growth factor I and insulin-like growth factor II increases gradually; Under the identical situation of concentration, the binding ability of AC122-1 is superior to the binding ability of AC122.Can find out that therefrom AC122-1 is a preferred embodiments of the present invention.
Embodiment 2:
Present embodiment is that example describes with the MCF-7 breast cancer cell.The MCF-7 cell is inoculated on the complete growth medium of one 6 orifice plate with 1.0 * 106 every holes.After the incubated overnight, with serum-free DMEM culture fluid cells washed, cultivated 6 hours at serum-free DMEM then, MCF-7 cell wherein can be in default of nutrient substance and death.With the reorganization Fab of variable concentrations or IgG cultured cell 30 minutes, add 1.5nM then and contain the insulin-like growth factor I of AC122-1 or insulin-like growth factor II that 10nM contains AC122-1 to culture medium.After 20 minutes, cell is placed cooled on ice, wash with cold poly-succinic fourth two fat; With 1ml lysis buffer [50mmol/L HEPES (pH 7.4); 150mmol/L NaCl, 10% glycerol, 1%Triton X-100; 1.5mmol/L MgCl2,2mmol/L vanadic acid sodium and protease inhibitor] carry out cracking.Lysate placed 30 minutes on ice, again in 17, and under the 000X g centrifugal 30 minutes.Collect supernatant and be used for immunoprecipitation, insulin like growth factor is separated out by immunity.Through after the deep washing, immunoprecipitation launches in 4% ~ 12% pay in advance on the albumin glue, transfers to PVDF membrane, and smears with anti-phosphorylation antibody 4610.In immunoprecipitation, film is stripped from, and detects total IGF-1 again with C-20 polyclonal antibody or C-19.
As shown in Figure 4; AC122-1 is in the MCF-7 breast cancer cell; The phosphorylation that can effectively suppress IGF-1 has reduced the information mediation of IGF-1, the cell proliferation activity of MCF-7 breast cancer cell is weakened even disappears.
Embodiment 3:
Present embodiment is that example describes with the MCF-7 breast cancer cell.Use the Transwell culture plate of the polycarbonate membrane in 8 μ m apertures, comprise the DMEM that 2.6ml has 5% hyclone and variable concentrations AC122-1 in the well of its bottom.With the DMEM of the DMEM and the serum-free that contain 5% hyclone respectively as the positive and negative control.The top is inserted and is comprised 0.5 * 10 6The serum-free DMEM 1.5ml of MCF-7 breast cancer cell single-cell suspension liquid.Cell is cultivated in 37 ℃ incubator.After four hours, wipe cell attached to the cell membrane upside with cotton swab.Cell to attached to the cell membrane downside dyes.Polycarbonate membrane is removed from transwell, be installed on the microscopical lantern slide, and carry out cell counting at microscopically.
As shown in Figure 5, AC122-1 is inhibited for the transfer of cancerous cell, and the AC122-1 of 40 nmol/L concentration can suppress in the culture medium of 5% hyclone the transfer of 40% MCF-7 breast cancer cell.
The method of the intravital tumor disease of treatment mammal of the present invention, its principle is not intended for a certain specific tumors disease.Use the method for the invention can realize treatment to tumor disease.Be that example has been enough to explain the therapeutic effect of the present invention to tumor disease with the MCF-7 breast cancer cell in the description.To other tumor disease describe can not be regarded as of the present invention disclose insufficient.
SEQUENCE LISTING
< 110>Sichuan remittance space pharmaceutical Co. Ltd
< 120>a kind of method of treating tumor disease in the mammalian body
< 130>a kind of method of treating tumor disease in the mammalian body
<160> 8
<170> PatentIn version 3.3
<210> 1
<211> 121
<212> PRT
<213> AC112 VH
<400> 1
Gln Val Gln Leu Val Gln Ser Gly Val Glu Val Lys Lys Pro Gly Ala
1 5 10 15
Ser Val Lys Val Pro Cys Lys Ala Ser Gly Tyr Thr Phe Thr Ser Tyr
20 25 30
Tyr Met His Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met
35 40 45
Gly Ile Ile Asn Pro Ser Gly Gly Ser Thr Ser Tyr Ala Gln Lys Phe
50 55 60
Gln Gly Arg Val Thr Met Thr Arg Asp Thr Ser Thr Ser Thr Val Tyr
65 70 75 80
Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Val Tyr Tyr Cys
85 90 95
Ala Arg Asp Asp Phe Trp Ser Gly Ala Val Gly Met Asp Val Trp Gly
100 105 110
Gln Gly Thr Thr Val Thr Val Ser Ser
115 120
<210> 2
<211> 110
<212> PRT
<213> AC112 VL
<400> 2
Asp Ile Gln Met Thr Gln Ser Pro Ala Thr Leu Ser Leu Ser Pro Gly
1 5 10 15
Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Asp Val Gly Ser Asp
20 25 30
Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro Arg Leu Leu Val
35 40 45
Ser Asp Ala Ser Asn Arg Ala Thr Gly Ile Pro Ala Arg Phe Ser Gly
50 55 60
Ser Gly Ser Gly Thr Asp Phe Lys Leu Thr Ile Asn Ser Leu Glu Pro
65 70 75 80
Glu Asp Ser Ala Val Tyr Tyr Cys Gln Gln Arg Arg Arg Trp Pro Pro
85 90 95
Gly Ala Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys Arg
100 105 110
<210> 3
<211> 120
<212> PRT
<213> AC113 VH
<400> 3
Glu Val Gln Leu Val Gln Ser Gly Val Asp Val Lys Lys Pro Gly Ser
1 5 10 15
Ser Val Lys Val Ser Cys Lys Ala Ser Gly Gly Thr Phe Ser Ser Tyr
20 25 30
Ala Ile Ser Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met
35 40 45
Gly Gly Ile Ile Pro Ile Phe Gly Thr Ala Asn Tyr Ala Gln Lys Phe
50 55 60
Gln Gly Arg Val Thr Ile Thr Ala Asp Glu Ser Ala Ser Thr Ala Tyr
65 70 75 80
Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Val Tyr Tyr Cys
85 90 95
Ala Ser Gly Tyr Glu Gly Pro Leu Trp Ala Phe Asp Ile Trp Gly Gln
100 105 110
Gly Thr Met Val Thr Val Ser Ser
115 120
<210> 4
<211> 112
<212> PRT
<213> AC113 VL
<400> 4
Gln Ala Ser Gln Ser Val Leu Thr Gln Pro Pro Ser Val Ser Ala Ala
1 5 10 15
Pro Gly Gln Arg Val Ser Ile Ser Cys Ser Gly Ser Ser Ser Asn Ile
20 25 30
Gly Asn Tyr His Val Ser Trp Tyr Gln His Leu Pro Gly Arg Ala Pro
35 40 45
Lys Leu Leu Ile Tyr Asp Asn Ser Lys Arg Pro Ser Gly Ile Pro Asp
50 55 60
Arg Phe Ser Gly Ser Lys Ser Gly Thr Ser Ala Thr Leu Asp Ile Thr
65 70 75 80
Gly Leu Gln Thr Gly Asp Glu Gly Asp Tyr Tyr Cys Ala Thr Trp Asp
85 90 95
Thr Ser Leu Arg Trp Val Phe Gly Thr Gly Thr Lys Val Thr Val Leu
100 105 110
<210> 5
<211> 120
<212> PRT
<213> AC122 VH
<400> 5
Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ser
1 5 10 15
Ser Val Lys Val Ser Cys Lys Ala Ser Gly Gly Thr Phe Ser Ser Tyr
20 25 30
Ala Ile Ser Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met
35 40 45
Gly Gly Ile Ile Pro Ile Leu Gly Ile Ala Asn Tyr Ala Gln Lys Phe
50 55 60
Gln Gly Arg Val Thr Ile Thr Ala Asp Glu Ser Thr Ser Thr Ala Tyr
65 70 75 80
Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Val Tyr Tyr Cys
85 90 95
Ala Arg Gly Pro Arg Gly Tyr Ser Tyr Asn Phe Asp Tyr Trp Gly Gln
100 105 110
Gly Thr Leu Val Thr Val Ser Ser
115 120
<210> 6
<211> 108
<212> PRT
<213> AC122 VL
<400> 6
Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly
1 5 10 15
Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Ser Ile Ser Ser Tyr
20 25 30
Leu Asn Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile
35 40 45
Tyr Ala Ala Ser Ser Leu Gln Ser Gly Val Pro Ser Arg Phe Ser Gly
50 55 60
Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro
65 70 75 80
Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Ser Tyr Ser Thr Pro Ser
85 90 95
Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys Arg
100 105
<210> 7
<211> 120
<212> PRT
<213> AC122-1 VH
<400> 7
Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ser
1 5 10 15
Ser Val Lys Val Ser Cys Lys Ala Ser Gly Gly Thr Phe Ser Ser Tyr
20 25 30
Ala Ile Ser Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met
35 40 45
Gly Gly Ile Ile Pro Ile Leu Gly Ile Ala Asn Tyr Ala Gln Lys Phe
50 55 60
Gln Gly Arg Val Thr Ile Thr Ala Asp Glu Ser Thr Ser Thr Ala Tyr
65 70 75 80
Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Val Tyr Tyr Cys
85 90 95
Ala Arg Gly Pro Arg Gly Tyr Ser Tyr Asn Phe Asp Tyr Trp Gly Gln
100 105 110
Gly Thr Leu Val Thr Val Ser Ser
115 120
<210> 8
<211> 108
<212> PRT
<213> AC122-1 VL
<400> 8
Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly
1 5 10 15
Asp Arg Val Thr Ile Ala Cys Arg Ala Ser Gln Thr Ile Ser Arg Tyr
20 25 30
Leu Asn Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile
35 40 45
Tyr Ala Ala Ser Ser Leu Gln Ser Gly Val Ser Ser Arg Phe Ser Gly
50 55 60
Ser Gly Ser Gly Thr Glu Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro
65 70 75 80
Glu Asp Phe Ala Thr Tyr Phe Cys Gln Gln Thr Tyr Ser Pro Pro Ile
85 90 95
Thr Phe Gly Gln Gly Thr Arg Leu Glu Ile Lys Arg
100 105

Claims (5)

1. method of treating tumor disease in the mammalian body is characterized in that it comprises:
Give medicine to mammal main body;
Described medicine comprises antibody, contains SEQ ID NO:1 in the described antibody, SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, the aminoacid sequence of putting down in writing among SEQ ID NO:7 or the SEQ ID NO:8;
Be attached on the insulin-like growth factor I to described antibody specificity, can reduce or eliminate the intravital tumor disease of mammal.
2. method according to claim 1 is characterized in that: be attached on the insulin-like growth factor II to described antibody specificity.
3. method according to claim 1 is characterized in that: described tumor disease is solid tumor, hematologic malignancies, leukemia, colorectal cancer, optimum or malignant breast carcinomas, uterus carcinoma, hysteromyoma, ovarian cancer, carcinoma of endometrium, polycystic ovary syndrome, endometrial polyp, carcinoma of prostate, prostate hyperplasia, hypophysis cerebri cancer, adenomyosis, adenocarcinoma, meningioma, melanoma, bone tumor, multiple myeloma, central nervous system cancer, glioma or astroblast cancer.
4. method according to claim 4 is characterized in that: described tumor disease is meant that the intravital tumor cell of described mammal shifts.
5. method according to claim 5 is characterized in that: described tumor disease is meant the intravital Metastasis in Breast Cancer of described mammal.
CN2012102878596A 2012-08-14 2012-08-14 Method for treating neoplastic disease in body of mammals Pending CN102793922A (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
CN2012102878596A CN102793922A (en) 2012-08-14 2012-08-14 Method for treating neoplastic disease in body of mammals

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
CN2012102878596A CN102793922A (en) 2012-08-14 2012-08-14 Method for treating neoplastic disease in body of mammals

Publications (1)

Publication Number Publication Date
CN102793922A true CN102793922A (en) 2012-11-28

Family

ID=47193388

Family Applications (1)

Application Number Title Priority Date Filing Date
CN2012102878596A Pending CN102793922A (en) 2012-08-14 2012-08-14 Method for treating neoplastic disease in body of mammals

Country Status (1)

Country Link
CN (1) CN102793922A (en)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2016533721A (en) * 2013-10-11 2016-11-04 アメリカ合衆国 TEM8 antibody and use thereof

Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN1620468A (en) * 2002-01-18 2005-05-25 皮埃尔法布雷医药公司 Novel anti-igf-ir antibodies and uses thereof
CN101578297A (en) * 2006-04-07 2009-11-11 美国政府健康及人类服务部 Antibody compositions and methods for treatment of neoplastic disease

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN1620468A (en) * 2002-01-18 2005-05-25 皮埃尔法布雷医药公司 Novel anti-igf-ir antibodies and uses thereof
CN101578297A (en) * 2006-04-07 2009-11-11 美国政府健康及人类服务部 Antibody compositions and methods for treatment of neoplastic disease

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2016533721A (en) * 2013-10-11 2016-11-04 アメリカ合衆国 TEM8 antibody and use thereof

Similar Documents

Publication Publication Date Title
Hendriks et al. Antibody-based cancer therapy: successful agents and novel approaches
CN102634486B (en) GPC3 (glypican-3) monoclonal antibody hybridoma cell strain 7D11 and preparation method and application thereof
US20240277803A1 (en) Nme inhibitors and methods of using nme inhibitors
Campos et al. Endothelial derived factors inhibit anoikis of head and neck cancer stem cells
KR102276489B1 (en) Improved anti-VEGFR-2 monoclonal antibody
EA023665B1 (en) c-Kit ANTIBODIES AND USES THEREOF
CN102268089A (en) AGR2 (Anterior Gradient-2) blocking antibody and application thereof
JP7514765B2 (en) Bispecific antibodies against human PD-L1 and PD-L2 and methods of use thereof
Ma et al. Synergistic effect of SCF and G-CSF on stem-like properties in prostate cancer cell lines
CN106866823A (en) A kind of nano antibody of anti-Her2
CN102020717A (en) Active factor for enhancing lymphocyte targeting killing tumors and preparation method thereof
CN102793922A (en) Method for treating neoplastic disease in body of mammals
CN104530236B (en) A kind of full people source HER2 antibody, its encoding gene and application
CN103360497A (en) Novel antitumor fusion protein vaccine, and preparation method and application thereof
CN111378036A (en) A kind of preparation method and application of anti-human leukemia inhibitory factor monoclonal antibody
CN110903402A (en) A kind of bispecific fusion protein and its construction method and application
CN103215292A (en) Human Pcid2 protein soluble expression method, anti-human Pcid2 protein monoclonal antibody 2D7-F11, and hybridoma cell line secreting antibody
WO2024001669A9 (en) Antibodies targeting itga2 and antibody-drug conjugates comprising same
KR20140073215A (en) A composition and a kit for seperating a cell, and a method for seperating a cell using the same
CN111333732B (en) Preparation and application of a bispecific antibody targeting human BCMA and activating NK cells
CN103555668A (en) Hybridoma cell strain and anti-Wnt5a monoclonal antibody produced thereby as well as application thereof
CN102504026A (en) Full human single chain antibody capable of resisting epidermal growth-factor receptor and application thereof
CN105886475B (en) Monoclonal antibody of catalytic subunit of DNA-dependent protein kinase and application
Hatzidaki et al. Novel antibody against TMX2 and its effects on breast cancer cells
Lin et al. Expression of intracellular domain of epidermal growth factor receptor and generation of its monoclonal antibody

Legal Events

Date Code Title Description
C06 Publication
PB01 Publication
C10 Entry into substantive examination
SE01 Entry into force of request for substantive examination
C12 Rejection of a patent application after its publication
RJ01 Rejection of invention patent application after publication

Application publication date: 20121128