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Protein Binders for Characterisation of Human Proteome Function: Generation, Validation, Application

Protein Binders for Characterisation of Human Proteome Function: Generation, Validation, Application

Objective

The Affinomics programme aims to leverage existing efforts in Europe to generate large-scale resources of validated protein-binding molecules (‘binders’) as affinity reagents for characterisation of the human proteome and to apply them in comprehensive structural and functional analyses of protein expression, interactions and complexes. Proteome targets will be focused on five categories of inter-related human proteins involved in signal transduction, cell regulation and cancer, namely protein kinases, SH2 domain-containing proteins, protein tyrosine phosphatases, proteins somatically mutated in cancers and candidate cancer biomarkers. Binders to about 1000 protein targets will be made over the course of the programme. A high throughput, coordinated production pipeline for antigens and binders will be established. Target antigens will be expressed in three forms, as folded full-length proteins or domains, as large peptide fragments (PrESTs) based on low homology to other human proteins and as small peptides, in some cases phosphorylated. Binder types to be generated include affinity-purified polyclonal antibodies, monoclonal antibodies, recombinant antibody fragments and non-immunoglobulin scaffolds. An important aspect will be the development of highly efficient ‘next generation’ recombinant selection methods, based on phage, cell and ribosome display, capable of producing high quality binders at greater throughput and lower cost than hitherto. Systems and procedures for thorough binder validation and quality control will be established. The affinity reagents will be applied in advanced innovative and sensitive technologies for specific detection of target proteins and interacting protein complexes in cells, tissues and fluids, for improved understanding of protein function and new classes of diagnostic assays.

Coordinator

THE BABRAHAM INSTITUTE

Address

Babraham Hall
Cb22 3at Cambridge

United Kingdom

Activity type

Higher or Secondary Education Establishments

EU Contribution

€ 823 536

Administrative Contact

Fang Gao (Mrs.)

Participants (19)

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KUNGLIGA TEKNISKA HOEGSKOLAN

Sweden

EU Contribution

€ 1 909 515

UNIVERSITAT ZURICH

Switzerland

EU Contribution

€ 1 125 484

LUNDS UNIVERSITET

Sweden

EU Contribution

€ 695 742

KOBENHAVNS UNIVERSITET

Denmark

EU Contribution

€ 727 600

TEKNOLOGIAN TUTKIMUSKESKUS VTT

Finland

EU Contribution

€ 459 007

EUROPEAN MOLECULAR BIOLOGY LABORATORY

Germany

EU Contribution

€ 454 400

UNIVERSITA DEGLI STUDI DI ROMA TOR VERGATA

Italy

EU Contribution

€ 398 282

BABRAHAM BIOSCIENCE TECHNOLOGIES LIMITED

United Kingdom

EU Contribution

€ 220 672

TECHNISCHE UNIVERSITAET BRAUNSCHWEIG

Germany

EU Contribution

€ 565 664

UNIVERSITAET KASSEL

Germany

EU Contribution

€ 426 579

HELMHOLTZ ZENTRUM MUENCHEN DEUTSCHES FORSCHUNGSZENTRUM FUER GESUNDHEIT UND UMWELT GMBH

Germany

EU Contribution

€ 131 571

Structural Genomics Consortium

United Kingdom

DEUTSCHES KREBSFORSCHUNGSZENTRUM HEIDELBERG

Germany

EU Contribution

€ 540 358

VIB

Belgium

EU Contribution

€ 505 473

KAROLINSKA INSTITUTET

Sweden

EU Contribution

€ 290 763

THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD

United Kingdom

EU Contribution

€ 290 763

EBERHARD KARLS UNIVERSITAET TUEBINGEN

Germany

EU Contribution

€ 374 014

UPPSALA UNIVERSITET

Sweden

EU Contribution

€ 670 293

PARATOPES LIMITED

United Kingdom

EU Contribution

€ 390 284

Project information

Grant agreement ID: 241481

Status

Closed project

  • Start date

    1 April 2010

  • End date

    31 March 2015

Funded under:

FP7-HEALTH

  • Overall budget:

    € 14 620 568,35

  • EU contribution

    € 11 000 000

Coordinated by:

THE BABRAHAM INSTITUTE

United Kingdom