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Affibody molecule-mediated depletion of HSA and IgG using different buffer compositions: a 15 min protocol for parallel processing of 1-48 samples
KTH, School of Biotechnology (BIO), Proteomics.
KTH, School of Biotechnology (BIO), Proteomics.ORCID iD: 0000-0001-8141-8449
KTH, School of Biotechnology (BIO).
KTH, School of Biotechnology (BIO), Proteomics.ORCID iD: 0000-0003-0605-8417
2010 (English)In: Biotechnology and applied biochemistry, ISSN 0885-4513, E-ISSN 1470-8744, Vol. 56, 49-57 p.Article in journal (Refereed) Published
Abstract [en]

High-abundant plasma proteins pose a challenge in a large number of proteomics-based technologies. Depletion of these high-abundant proteins has proven to be a fruitful strategy to circumvent masking of lower-abundant proteins that could serve as valuable biomarker candidates. However, current strategies often do not meet the throughput requirements of large-scale proteomic studies. In the present paper, a flexible and parallelized method for the depletion of high-abundant proteins is described, allowing the removal of the two most abundant proteins from 48 blood-derived samples in less than 15 min using Affibody molecules as affinity ligands. A sample-processing platform like this should be suitable for a number of proteomics technologies; its flexibility in buffer composition allows for different types of downstream applications.

Place, publisher, year, edition, pages
2010. Vol. 56, 49-57 p.
Keyword [en]
Affibody molecule, human serum albumin (HSA), IgG, protein depletion, high throughput analysis, sample preparation, serum or plasma analysis
National Category
Industrial Biotechnology
URN: urn:nbn:se:kth:diva-29471DOI: 10.1042/BA20100041ISI: 000280262400002ScopusID: 2-s2.0-77954833249OAI: diva2:395828
Swedish Research CouncilKnut and Alice Wallenberg Foundation
QC 20110208Available from: 2011-02-08 Created: 2011-02-02 Last updated: 2011-02-08Bibliographically approved

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Eriksson, CeciliaSchwenk, Jochen M.Hober, Sophia
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