A kind of ildr2 antibody, its pharmaceutical composition and use thereof

A technology of antibodies and drugs, applied in the field of pharmaceutical compositions, can solve the problem of no progression of rheumatoid arthritis

Active Publication Date: 2021-12-31
康旭生物科技(深圳)有限公司
View PDF4 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

The above drugs have a certain effect on the treatment of rheumatoid arthritis, but generally there is no effective drug to control the pathogenesis of rheumatoid arthritis

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • A kind of ildr2 antibody, its pharmaceutical composition and use thereof
  • A kind of ildr2 antibody, its pharmaceutical composition and use thereof
  • A kind of ildr2 antibody, its pharmaceutical composition and use thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0025] Example 1: Obtaining novel ILDR2 chimeric antibodies

[0026] For mouse immunization, 6- to 8-week-old female BALB / c mice (purchased from Shanghai Jiake Biotechnology Co., Ltd.) were used as experimental animals, and 50 μg of human ILDR2 protein (purchased from Beijing Yiqiao Shenzhou Biotechnology Co., Ltd.) was used for the first immunization Mix well with complete Freund's adjuvant to form an emulsion, inject 0.5ml / mouse intraperitoneally into mice, and carry out booster immunization every 2 weeks, use 25 μg of human ILDR2 protein to fully mix with incomplete Freund's adjuvant to form an emulsion for booster immunization, Inject 0.5ml / mouse intraperitoneally into the mouse, boost immunization 3 times, take the venous blood of the mouse and separate the serum one week after the last immunization, measure the titer of the obtained antibody by ELISA method, and select the mouse cells with high titer to prepare Single splenocyte suspensions were prepared from hybridomas....

Embodiment 2

[0031] Example 2: Detection of anti-human ILDR2 chimeric monoclonal antibody

[0032] Detect the kinetic constant of the anti-human ILDR2 chimeric monoclonal antibody (hereinafter referred to as Anti-ILDR2-M) obtained in Example 1 and its antigen binding, and use the instrument optical surface plasmon resonance technology to detect the molecules coupled and coated on the biochip Binding and dissociation with the analyte molecule. Specifically, Anti-ILDR2-M was dissolved in a sodium acetate buffer solution (pH 5.0) and coupled to a CM chip, followed by blocking with 1M ethanolamine. In the binding phase, different concentrations of Anti-ILDR2-M were injected at a speed of 30 μL / min for 3 min, and in the dissociation phase, PBS buffer solution was injected at a speed of 30 μL / min for 10 min, and the binding kinetic constant and dissociation kinetic constant were passed Biacore3000 software was used for analysis and calculation. The binding kinetic constants, dissociation kinet...

Embodiment 3

[0037] Example 3: Preparation of novel humanized ILDR2 antibody

[0038] The humanized form of anti-human ILDR2 antibody was prepared by referring to the preparation method of Molecule Immunol, and the humanized template that best matched the Anti-ILDR2-M non-CDR region was selected from the Germline database, and the template of the heavy chain variable region was human IgVH4-28*03, the template of the variable region of the light chain is human IGKV1-16*02, the CDR region of the mouse antibody is grafted onto the selected humanized template, and the CDR region of the human template is replaced to obtain the heavy chain of the humanized antibody For the variable region, the amino acid sequence is shown in SEQ ID NO:7, and the light chain variable region of the humanized antibody is obtained, and the amino acid sequence is shown in SEQ ID NO:8. The amino acid sequence (VH) of the variable region of the heavy chain (VH) and the amino acid sequence (VL) of the variable region of...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

No PUM Login to view more

Abstract

A monoclonal antibody or an antigen-binding fragment thereof against Ig-like domain receptor 2 (ILDR2) is provided, the monoclonal antibody can specifically bind to ILDR2, and can effectively inhibit its ILDR2 immune function, and the present invention also provides Provides a pharmaceutical composition comprising the monoclonal antibody and its use, the pharmaceutical composition has the ability to prepare and assist in the treatment of rheumatoid arthritis, osteoarthritis, ankylosing spondylitis, psoriatic arthritis, and systemic sclerosis , systemic lupus erythematosus, Crohn's disease, drug potential for allergic asthma.

Description

technical field [0001] The present invention relates to the field of pharmaceutical compositions, in particular to an ILDR2 antibody, its pharmaceutical composition and its use. Background technique [0002] Rheumatoid arthritis (RA) is a chronic systemic disease of unknown etiology mainly characterized by inflammatory synovitis. It is characterized by polyarticular, symmetrical, and aggressive arthritis of the small joints of the hands and feet, often accompanied by involvement of extra-articular organs and positive serum rheumatoid factor, which can lead to joint deformities and loss of function. [0003] The pathogenesis of rheumatoid arthritis may be related to heredity, infection, sex hormones, etc. The pathology of rheumatoid arthritis mainly includes the proliferation of synovial lining cells, the infiltration of a large number of inflammatory cells in the interstitium, the neogenesis of microvessels, the formation of pannus, and the formation of cartilage and Destru...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
Patent Type & Authority Patents(China)
IPC IPC(8): C07K16/18A61K39/395A61P29/00A61P19/02A61P19/08A61P17/06A61P11/06A61P37/08A61P17/00A61P37/02A61P1/00
CPCC07K16/18A61P29/00A61P19/02A61P19/08A61P17/06A61P11/06A61P37/08A61P17/00A61P37/02A61P1/00A61K2039/505C07K2317/56C07K2317/565
Inventor 蒋可
Owner 康旭生物科技(深圳)有限公司
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap