Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Antibody to human epo receptor

By developing antibodies that specifically bind to phosphotyrosyl residues, the problem that existing technology cannot distinguish between non-activated and activated EPO-R is solved, accurate analysis of the activation status of EPO-R is achieved, and diagnosis and research are improved. accuracy.

Inactive Publication Date: 2011-12-14
F HOFFMANN LA ROCHE & CO AG
View PDF5 Cites 1 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, at the currently known state of the art, known antibodies against EPO-R are not able to distinguish between inactive and activated EPO-R (see Jelkmann, W. et al., Crit. Rev. Onc / Hematol. 67 (2008 ) 39-61; Li, K. et al., J. Biol. Chem. 278 (2003) 40702-40709, and Wu, H. et al., Proc. Natl. Acad. Sci. USA 94 (1997) 1806-1810 )

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
  • Antibody to human epo receptor
  • Antibody to human epo receptor
  • Antibody to human epo receptor

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0027] The term "antibody" encompasses various forms of antibody structures including, but not limited to, whole antibodies and antibody fragments.

[0028] An "antibody fragment" comprises a portion of a full-length antibody, preferably its variable domain, or at least its antigen-binding site. Examples of antibody fragments include diabodies, single chain antibody molecules, and multispecific antibodies formed from antibody fragments. scFv antibodies are described, eg, in Houston, J.S., Methods Enzymol. 203 (1991) 46-88. In addition, antibody fragments contain V H domain (i.e. capable of interacting with V L domain co-assembly) or V that binds EPO-R L domain (i.e. capable of interacting with V H Domains are assembled together as a single-chain polypeptide characteristic of a functional antigen-binding site), thereby providing an antibody with specific binding properties to human EPO-R.

[0029]The term "humanized antibody" refers to an antibody whose framework and / or "c...

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

PropertyMeasurementUnit
composition ratioaaaaaaaaaa
composition ratioaaaaaaaaaa
Login to View More

Abstract

An antibody binding to human EPO-R, characterized in specifically binding pY461, pY430 or p465 is useful for the determination of activated EPO receptor.

Description

Background of the invention [0001] Human erythropoietin (EPO) is a 166-aa glycoprotein involved in the proliferation and differentiation of erythroid progenitors. These cellular responses are mediated by the human EPO receptor (EPO-R), a 508-aa glycoprotein. The human EPO receptor (EPO-R) is a 508 amino acid long protein (Swiss Prot P19235) that contains a single transmembrane domain and has been classified as a member of the growth hormone subfamily of type I cytokine receptors. EPO-R is described eg in Winkelmann, J.C. et al., Blood 76 (1990) 24-30 and Jones, S.S. et al., Blood 76 (1990) 31-35). Activation of EPO-R occurs through dimerization (Matthews, D.J., PNAS 93 (1996) 9471-9476). EPO-R contains eight cytoplasmic tyrosine sites that are phosphorylated after stimulation with EPO (Li, K. et al., J. Biol. Chem. 278 (2003) 40702-40709; Wu, H. et al. , Proc. Natl. Acad. Sci. USA 94 (1997) 1806-1810), leading to "activated EPO-R". [0002] Anti-EPO-R antibodies are descri...

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 Applications(China)
IPC IPC(8): C07K16/28C07K16/44
CPCC07K2317/34C07K2317/565C07K16/2863C07K2317/56C07K16/44
Inventor M·雅尔斯M·库比斯O·穆恩迪格尔N·托莱斯-纳格尔
Owner F HOFFMANN LA ROCHE & CO AG
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

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

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com