Please use this identifier to cite or link to this item: https://doi.org/10.1007/978-1-61779-573-2_13
DC FieldValue
dc.title2D DIGE analysis of serum after fractionation by proteominer™ beads
dc.contributor.authorLiang, C.
dc.contributor.authorTan, G.S.
dc.contributor.authorChung, M.C.M.
dc.date.accessioned2014-11-26T07:42:15Z
dc.date.available2014-11-26T07:42:15Z
dc.date.issued2012
dc.identifier.citationLiang, C.,Tan, G.S.,Chung, M.C.M. (2012). 2D DIGE analysis of serum after fractionation by proteominer™ beads. Methods in Molecular Biology 854 : 181-194. ScholarBank@NUS Repository. <a href="https://doi.org/10.1007/978-1-61779-573-2_13" target="_blank">https://doi.org/10.1007/978-1-61779-573-2_13</a>
dc.identifier.isbn9781617795725
dc.identifier.issn10643745
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/109134
dc.description.abstractSerum is a popular biofluid used for many protein biomarker discovery projects since the collection and processing of serum/plasma is relatively noninvasive and inexpensive. Unfortunately, the downstream analysis of serum/plasma is hampered severely by several high-abundant proteins which often interfere with the separation and detection of many of the proteins of lower abundance. Thus, a number of prefractionation methods have recently been developed with the view to reduce the dynamic range of these proteins. These include both dye- and immunoaffinity-based methods that are specifically designed to remove serum albumin. In this chapter, we describe an alternative method using ProteoMiner™ or Equalizer beads that is aimed at overcoming this problem in serum. This method uses a combinatorial library of hexapeptides bound to beads and works by binding proteins until saturation is reached. Thus, the high-abundant proteins will reach saturation quickly, while the lower-abundant proteins continue to bind. This results in a dramatic depletion of the most abundant proteins, with a concurrent concentration of the middle- to low-abundant proteins. © 2012 Springer Science+Business Media, LLC.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1007/978-1-61779-573-2_13
dc.sourceScopus
dc.subject2D DIGE
dc.subjectEqualizer beads
dc.subjectProteoMiner™
dc.subjectSerum
dc.typeArticle
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.contributor.departmentBIOCHEMISTRY
dc.description.doi10.1007/978-1-61779-573-2_13
dc.description.sourcetitleMethods in Molecular Biology
dc.description.volume854
dc.description.page181-194
dc.identifier.isiutNOT_IN_WOS
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

6
checked on Aug 18, 2019

Page view(s)

159
checked on Aug 16, 2019

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.