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PROT20LC

Millipore

ProteoPrep® 20 Plasma Immunodepletion LC Column

Synonym(e):

ProteoPrep® 20

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About This Item

UNSPSC-Code:
12352200

Lagertemp.

2-8°C

Allgemeine Beschreibung

Discover protein biomarkers faster with the ProteoPrep20 LC Column! The ProteoPrep20 LC Column removes 20 highly abundant proteins (representing 97% of the proteome) from human plasma or serum, revealing biologically significant biomarkers previously masked. These twenty proteins are depleted at an average efficiency of 98% (albumin and IgG at >99% and the remaining 18 proteins at >85%). The depleted, biologically significant remaining proteins can then be concentrated at least 20-fold.

The ProteoPrep20 LC Column can accommodate a plasma or serum sample of 100 microliters, and will deplete 100 samples or more. This effectively enables immunodepletion of 10,000 microliters of plasma or serum.

The ProteoPrep20 LC Column is designed for use with low or medium pressure liquid chromatography systems. With minor system modifications, it can also be used with high pressure liquid chromatography systems. To learn more about using the ProteoPrep20 LC Column with an HPLC system, consult the User Guide.

The ProteoPrep20 LC Column specifically depletes the following plasma proteins:
Albumin
IgG
Transferrin
Fibrinogen
IgA
α2- Marcroglobulin
IgM
α1- Antitrypsin
Complement C3
Haptoglobulin
Apolipoprotein A1
Apolipoprotein A2
Apolipoprotein B
α1- Acid Glycoprotein
Ceruloplasmin
Complement C4
Complement C1q
IgD
Prealbumin
Plasminogen

Anwendung

Proteoprep 20 is an immunodepletion liquid chromatography (LC) column that removes 20 abundant interferring proteins from plasma or serum to allow analysis of less abundant proteins. Proteoprep 20 removes: albumin, IgG, transferrin, fibrinogen, IgA, α2- Marcroglobulin, IgM, α1- Antitrypsin, complement C3, haptoglobulin, apolipoprotein A1, A3 and B; α1- Acid Glycoprotein, ceruloplasmin, complement C4, C1q; IgD, prealbumin, and plasminogen.

Leistungsmerkmale und Vorteile

Discover the ProteoPrep20 LC Column for yourself!
  • Reduce sample complexity and increase efficiency by removing 20 highly abundant proteins
  • Reveal proteins previously masked
  • Enrich proteins of interest up to 20-fold

Rechtliche Hinweise

ProteoPrep is a registered trademark of Merck KGaA, Darmstadt, Germany

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Thomas Linke et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 849(1-2), 273-281 (2006-12-26)
The proteomic analysis of plasma and serum samples represents a formidable challenge due to the presence of a few highly abundant proteins such as albumin and immunoglobulins. Detection of low abundance protein biomarkers requires therefore either the specific depletion of
Tatiana Plavina et al.
Journal of proteome research, 6(2), 662-671 (2007-02-03)
We report on the development of a robust and relatively high-throughput method for in-depth proteomic analysis of human plasma suitable for biomarker discovery. The method consists of depletion of albumin and IgG and multi-lectin affinity chromatography (M-LAC), followed by nanoLC-MS/MS
Nitin Seam et al.
Clinical chemistry, 53(11), 1915-1920 (2007-09-25)
Prefractionation techniques such as serum albumin depletion are useful precursors to proteomic analysis, but they may introduce preanalytical bias if the depletion is not reproducible. We examined the reproducibility of albumin immunodepletion and describe a method of QC for this
Nicholas A Cellar et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 877(1-2), 79-85 (2008-11-29)
Proteomic analysis can be hampered by the large concentration distribution of proteins. Immunoaffinity techniques have been applied to selectively remove high abundant proteins (HAP's) from samples prior to analysis. Although immunodepletion of HAP's has been shown to enable greater detection
M K Disni R Dayarathna et al.
Journal of separation science, 31(6-7), 1156-1166 (2008-02-29)
Plasma is an important biological material for biomarker discovery. However, the wide dynamic range in protein concentration remains a major challenge. In this paper, we introduce the development of a proteomic platform for analysis of plasma samples. The method utilizes

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