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|Title:||2D DIGE analysis of serum after fractionation by proteominer™ beads||Authors:||Liang, C.
|Issue Date:||2012||Citation:||Liang, 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. https://doi.org/10.1007/978-1-61779-573-2_13||Abstract:||Serum 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.||Source Title:||Methods in Molecular Biology||URI:||http://scholarbank.nus.edu.sg/handle/10635/109134||ISBN:||9781617795725||ISSN:||10643745||DOI:||10.1007/978-1-61779-573-2_13|
|Appears in Collections:||Staff Publications|
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