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

Antibodies and immunoconjugates and uses therefor

A technology for antibodies and biological samples, applied in the direction of anti-animal/human immunoglobulin, anti-receptor/cell surface antigen/cell surface determinant immunoglobulin, non-active ingredient medical preparations, etc., can solve the problem of efficacy low level problem

Inactive Publication Date: 2009-07-22
GENENTECH INC
View PDF193 Cites 63 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

The conjugate was reported to be 200-fold less potent than the corresponding disulfide linker conjugate

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
  • Antibodies and immunoconjugates and uses therefor
  • Antibodies and immunoconjugates and uses therefor
  • Antibodies and immunoconjugates and uses therefor

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0984] Example 1: Preparation of mouse anti-human CD22 monoclonal antibody

[0985]A murine monoclonal antibody capable of specifically binding to human CD22 was prepared. Six-week-old BALB / c female mice were immunized in their paw pads with purified human CD22 plus his-8-tagged extracellular domain (SEQ ID NO: 30( ECD) at the C-terminus plus the sequence GRAHHHHHHHH) or the extracellular domain of CD22 plus his-8 tag comprising domains 1-7 (SEQ ID NO: 28 (ECD) plus the His sequence tag above). Subsequent injections were administered in the same manner one and three weeks after the initial immunization. Three days after the final injection, inguinal and popliteal lymph nodes were removed and pooled, and single cell suspensions were prepared by passing the tissue through a steel gauze. The cells were fused with mouse myeloma, such as P3X63-Ag8.653 (ATCCCRL1580), at a 4:1 ratio in high glucose (DMEM) containing 50% w / v polyethylene glycol 4000. Then with 2x10 5 Density per w...

Embodiment 2

[0988] Example 2: FACS-based assay for the analysis of anti-human CD22 monoclonal antibodies (MAbs)

[0989] CHO cells expressing human CD22 on their surface were incubated with anti-CD22 hybridoma supernatant in 100 μl FACS buffer (0.1% BSA in PBS, pH 7.4, 10 mM sodium azide) at 4° C. for 30 minutes, followed by Wash once with FACS buffer. The amount of anti-CD22 binding was determined by aliquots of the antibody / cell mixture with polyclonal FITC-conjugated goat or rabbit anti-mouse IgG (AccurateChem. Co., Westbury, NY) (for murine test antibody ) or goat or rabbit anti-human IgG (for humanized antibodies) were incubated at 4°C for 30 minutes, followed by three washes with FACS buffer.

Embodiment 3

[0990] Example 3: Preparation of humanized anti-CD22 antibody

[0991] A humanized 10F4 antibody was generated in which the hypervariable region (HVR) amino acid residues (interchangeably referred to as complementarity-determining regions) were modified by site-directed mutagenesis (Kunkel et al., Methods Enzymol. (1987), 154:367-382). or CDR) to obtain two variants, humanized 10F4v1 and humanized 10F4v2 (also referred to herein as "10F4v1" or "hu10F4v1" or "10F4v2" or "hu10F4v2", respectively). A third version, humanized 10F4v3 ("10F4v3" or "hu10Fv3") used in some of the studies disclosed herein, has the same mature protein light and heavy chain amino acid sequences as The expression vectors contain different signal sequences.

[0992] Humanization of the murine 10F4 antibody was performed as disclosed herein. Briefly, the light and heavy chain hypervariable regions of murine 10F4 were cloned into a modified consensus framework sequence to generate Figure 2A with 2B Amin...

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

Anti-CD22 antibodies and immunoconjugates thereof are provided. Methods of using anti-CD22 antibodies and immunoconjugates thereof are provided.

Description

[0001] This application is a non-provisional application filed pursuant to 37 CFR 1.53(b), U.S. Provisional Application Serial No. 60 / 809,328 filed May 30, 2006, and 60 filed March 29, 2007 pursuant to 35USC 119(e) / 908,941 and priority of 60 / 911,829 filed April 13, 2007, the entire contents of which applications are hereby incorporated by reference. technical field [0002] The present invention relates to anti-CD22 antibody and immunoconjugate thereof. The invention further relates to methods of using anti-CD22 antibodies and immunoconjugates thereof. Background technique [0003] Lymphocytes are one of many types of white blood cells produced in the bone marrow during hematopoiesis. There are two major classes of lymphocytes: B lymphocytes (B cells) and T lymphocytes (T cells). Lymphocytes of particular interest herein are B cells. [0004] B cells mature within the bone marrow, then exit the bone marrow and express antigen-binding antibodies on their cell surface. Wh...

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): C07K16/28A61K47/48A61K47/68
Inventor 小艾伦·J·埃本斯阿兰·M·格雷梁伟庆吴雁于尚凡
Owner GENENTECH INC
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