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Single framework recombinant antibody fragments designed for protein chip applications

Steinhauer, Cornelia LU ; Wingren, Christer LU ; Malmborg Hager, Ann-Christin LU and Borrebaeck, Carl LU (2002) In BioTechniques p.38-38
Abstract
High-throughput proteomics, based on the microarray platform, requires stable, highly functional components that will yield a highly sensitive read-out of low, abundance protein. Although antibodies are the best characterized binding molecules for this purpose, only a fraction of them appear to behave satisfactorily in the chip format. Therefore, high demands need to be placed on their molecular design. In the present study, we have focused an recombinant antibody design based on a single framework for protein chip applications, aiming at defining crucial molecular probe parameters. Our results show that engineered human recombinant scFv antibody fragment, that displayed appropriate biophysical properties (molecular [functional] stability... (More)
High-throughput proteomics, based on the microarray platform, requires stable, highly functional components that will yield a highly sensitive read-out of low, abundance protein. Although antibodies are the best characterized binding molecules for this purpose, only a fraction of them appear to behave satisfactorily in the chip format. Therefore, high demands need to be placed on their molecular design. In the present study, we have focused an recombinant antibody design based on a single framework for protein chip applications, aiming at defining crucial molecular probe parameters. Our results show that engineered human recombinant scFv antibody fragment, that displayed appropriate biophysical properties (molecular [functional] stability in particular) can be generated, making them prime candidates for high-density antibody arrays. In fact a superior framework that displays both multifaceted adsorption properties and very high functional stability over several months on chips (stored in a dried-out state) was identified Taken together designed scFv fragments based on a single molecular scaffold, readily accessible in Large phage display libraries, can undoubtedly meet the requirements of probe content in antibody microarrays, particularly for global proteome analysis. (Less)
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author
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Contribution to journal
publication status
published
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in
BioTechniques
issue
Suppl.
pages
38 - 38
publisher
Informa Healthcare
external identifiers
  • wos:000180064700006
  • scopus:0036908782
ISSN
0736-6205
language
English
LU publication?
yes
id
003d8432-8731-4e64-9a3a-1d9efabc4964 (old id 321105)
date added to LUP
2007-11-14 14:19:43
date last changed
2017-08-20 04:27:32
@article{003d8432-8731-4e64-9a3a-1d9efabc4964,
  abstract     = {High-throughput proteomics, based on the microarray platform, requires stable, highly functional components that will yield a highly sensitive read-out of low, abundance protein. Although antibodies are the best characterized binding molecules for this purpose, only a fraction of them appear to behave satisfactorily in the chip format. Therefore, high demands need to be placed on their molecular design. In the present study, we have focused an recombinant antibody design based on a single framework for protein chip applications, aiming at defining crucial molecular probe parameters. Our results show that engineered human recombinant scFv antibody fragment, that displayed appropriate biophysical properties (molecular [functional] stability in particular) can be generated, making them prime candidates for high-density antibody arrays. In fact a superior framework that displays both multifaceted adsorption properties and very high functional stability over several months on chips (stored in a dried-out state) was identified Taken together designed scFv fragments based on a single molecular scaffold, readily accessible in Large phage display libraries, can undoubtedly meet the requirements of probe content in antibody microarrays, particularly for global proteome analysis.},
  author       = {Steinhauer, Cornelia and Wingren, Christer and Malmborg Hager, Ann-Christin and Borrebaeck, Carl},
  issn         = {0736-6205},
  language     = {eng},
  number       = {Suppl.},
  pages        = {38--38},
  publisher    = {Informa Healthcare},
  series       = {BioTechniques},
  title        = {Single framework recombinant antibody fragments designed for protein chip applications},
  year         = {2002},
}