c-MET kinase binding proteins

An immunoglobulin and monomer technology, applied in the field of c-MET kinase-binding protein, can solve problems such as reducing tumorigenic potential

Inactive Publication Date: 2007-08-15
安姆根山景公司
View PDF18 Cites 7 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Second, downregulation of Met or HGF expression in h

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
  • c-MET kinase binding proteins
  • c-MET kinase binding proteins
  • c-MET kinase binding proteins

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0474] This example describes the selection of monomeric domains and the generation of multimers.

[0475] From any of a variety of human and / or non-human sequences, starting materials for identifying monomeric domains and generating multimers from selected monomeric domains and methods can be derived. For example, to produce selected monomeric domains with specific binding to a desired ligand or mixture of ligands, one or more monomeric domain genes are selected from families of monomeric domains that bind certain ligands. Nucleic acid sequences encoding one or more monomeric domain genes can be obtained by PCR amplification of genomic DNA or cDNA, or, optionally, can be produced synthetically using overlapping oligonucleotides.

[0476] Most commonly, these sequences are then cloned into a cell surface display format (ie bacterial, yeast or mammalian (COS) cell surface display; phage display) for expression and screening. The recombinant sequences are transfected (transduce...

Embodiment 2

[0481] This example describes in vivo in-protein recombination to generate a library of greater diversity

[0482] The monomer-encoding plasmid vector (pCK-derived vector; see below) flanked by orthologous loxP sites was recombined with the phage vector via its compatible loxP sites in a Cre-dependent manner. Recombinant phage vectors were detected by PCR using primers specific for the recombinant construct. DNA sequencing showed that the correct recombination product was produced.

[0483] Reagents and Experimental Methods

[0484] pCK-cre-lox-monomer-loxP. This vector has 2 particularly relevant features. First, it carries the P lac The cre gene under control encodes the site-specific DNA recombinase Cre. Cre was PCR-amplified from p705-cre (purchased from GeneBridges) with cre-specific primers, which incorporated XbaI (5') and SfiI (3') at the ends of the PCR product. The product was digested with XbaI and SfiI and cloned into the bla of pCK (pCK110919-HC-Bla (pACYC o...

Embodiment 6

[0518] This example describes the construction of an EGF-based monomer library.

[0519] CaEGF domain library E3 encodes a protein domain of 36-43 amino acids with the following pattern:

[0520] X(5)C1-X(4 / 6)-C2-X(4,5)-C3-X(8)-C4-X(1)-C5-X(8 / 12)-C6

[0521] The table below describes each position, which amino acid is encoded in a library based on the natural diversity of human calcium-binding EGF domains:

[0522]

[0523] A library E3 of DNA sequences encoding monomeric calcium-binding EGF domains was generated by assembly PCR as described by Stemmer et al., Gene 164:49-53 (1995). The oligonucleotides used in this PCR reaction were 2 sets, 1 and 2. They are:

[0524] Group 1:

[0525] 1.5'-AAAAGGCCTCGAGGGCCTGGGTGGCAATGGT-3'

[0526] 2.5'-CCTGAACCACCACAKHKACCGYKSNBGCACGGAYYCGRCRMACATTCATYAAYATCTDYACCATTGCCACCC-3'

[0527] 3.5'-CCTGAACCACCACAKNTGSCGYYGYKMHSGCACGGAYYCGRCRMACATTCATYAAYATCTDYACCATTGCCACCC-3'

[0528] 4.5'-CCTGAACCACCACAKHKACCGYKSNBGCAARBAYBCGVAHYCWSKBYA...

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
Titeraaaaaaaaaa
Login to view more

Abstract

Polypeptides comprising monomer domains that bind to c-MET, or portions thereof, are provided.

Description

[0001] Cross References to Related Applications [0002] This application is a continuation-in-part of U.S. Patent Application Serial No. 10 / 957,351, filed September 30, 2004, which is a continuation-in-part of U.S. Patent Application Serial No. 10 / 871,602, filed June 17, each of which discloses The entirety is incorporated by reference for all purposes. Background of the invention [0003] Hepatocyte growth factor / scatter factor (HGF / SF) is a mesenchymal-derived pleiotropic factor that regulates cell growth, cell motility, and morphogenesis of various cell types, and is involved in embryonic development and organogenesis In, mediates epithelial-mesenchymal interactions, the latter tissue interactions responsible for morphogenesis. Although HGF was originally identified as a potent mitogen for hepatocytes, it has also been identified as an angiogenic growth factor. [0004] Met was first identified as an oncogene in the 1980s and is a receptor for HGF. The proto-oncogene c-...

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): A61K38/00G01N33/53C07H21/02
CPCG01N2500/00A61K38/00G01N33/574C07K14/47
Inventor W·P·C·斯特默D·V·佩尔罗思S·萨特亚尔B·M·阿尔巴A·巴克A·N·杜瓜伊Q·刘J·西尔弗曼R·史密斯C·斯维默
Owner 安姆根山景公司
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