Humanized and de-immunized antibodies

A humanized antibody and antibody technology, applied in the field of humanized and deimmunized antibodies, can solve problems such as insufficient antibody, impossible to establish CMC production, and inability to establish stable cell clones

Pending Publication Date: 2020-09-15
维沃永治疗公众有限公司
View PDF27 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0037] However, with said clone #6 variant as disclosed in WO 2017/009459 it was not possible to establish CMC production
In particular, despite numerous attempts, it was not possible to establish a stable cell clon

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
  • Humanized and de-immunized antibodies
  • Humanized and de-immunized antibodies
  • Humanized and de-immunized antibodies

Examples

Experimental program
Comparison scheme
Effect test

Example Embodiment

[0332] Example

[0333] 1. To produce N3pE-Aβ specific antibody by humanization method

[0334] The humanized and deimmunized antibodies of the present invention are humanized and deimmunized forms of monoclonal mouse antibodies produced by the hybridoma cell line Aβ6-1-6 (Accession No. DSM ACC 2924), which hybridoma cells The line Aβ6-1-6 is described in WO2010 / 009987. Humanization was performed as described in WO 2017 / 009459. Working Example 1 disclosed on pages 58-60 of WO 2017 / 009459 is incorporated herein by reference.

[0335] 2. RNA Isolation and cDNA Synthesis

[0336] As a source of constant sequences, RNA from human B cells was isolated by lysing 500 [mu]l whole blood with 5 ml 1x FACS Lysis Buffer (Becton Dickinson) for 10 min at room temperature. The lysate was centrifuged at 300 g for 5 minutes; the pellet was washed twice with PBS and then dissolved in 350 μl Nucleo RNA II in RA1 buffer (Macherey-Nagel) and 3.5 μl of 0.5M TCEP (SIGMA) was added. Isolate RN...

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
Dissociation constantaaaaaaaaaa
Login to view more

Abstract

The invention relates to humanized and de-immunized antibodies that bind to an epitope at the N-terminus of pyroglutamated amyloid beta (A beta N3pE) peptide and to preventive and therapeutic treatment of diseases and conditions that are related to accumulation and deposition of amyloid peptides, such as amyloidosis, a group of disorders and abnormalities associated with pyroglutamated amyloid peptide, like Alzheimer's disease, Down's syndrome, cerebral amyloid angiopathy and other related aspects. More specifically, it pertains to the use of monoclonal antibodies of the invention to bind pyroglutamated amyloid beta peptide in plasma, brain, and cerebrospinal fluid to prevent accumulation or to reverse deposition of A beta N3pE within the brain and in various tissues in the periphery, andto alleviate amyloidosis. The present invention further pertains to diagnostic assays for the diagnosis of amyloidosis using the antibodies of the invention.

Description

technical field [0001] The present invention relates to humanized and de-immunized antibodies that bind to an epitope at the N-terminus of the pyroglutamated amyloid beta (AβN3pE) peptide and also to diseases and disorders Preventive and therapeutic treatment of diseases and conditions associated with the accumulation and deposition of amyloid peptides, such as amyloidosis (a group of disorders and abnormalities associated with pyroglutamated amyloid peptides, such as Alzheimer's disease, Down syndrome, cerebral amyloid angiopathy, and other related aspects). More specifically, it relates to the use of monoclonal antibodies of the present invention to bind pyroglutamate-amyloid beta peptide in plasma, brain and cerebrospinal fluid to prevent or reverse the accumulation of AβN3pE in various tissues in and around the brain and to alleviate Use in amyloidosis. The invention also relates to diagnostic assays for the diagnosis of amyloidosis using the antibodies of the invention....

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
IPC IPC(8): C07K16/18
CPCC07K16/18C07K2317/24C07K2317/71C07K2317/92C07K2317/94A61P25/28A61K2039/505A61K47/06C07K16/00C07K2317/565
Inventor J-U·拉费尔德S·吉利斯T·赫特曼S·席林M·克莱因施密特
Owner 维沃永治疗公众有限公司
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