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SEP080

Millipore

Seppro® Rubisco

LC2

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

column D × L

6.4 mm × 63 mm

capacity

1 mg total protein loading(D-Ribulose 1,5-Diphosphate Carboxylase (Rubisco))

storage temp.

2-8°C

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General description

RuBisCO (Ribulose-1,5-bisphosphate carboxylase/oxygenase) is the most abundant protein in plants, and it may be the most abundant protein on Earth. RuBisCO is an enzyme that is used in the Calvin cycle to catalyze the first major step of carbon fixation, a process by which the atoms of atmospheric carbon dioxide are made available to organisms in the form of energy-rich molecules such as sucrose. RuBisCO, while being the key enzyme in photosynthetic carbon assimilation in green leaves, is the main obstacle in plant proteomics. It constitutes about 40% of the total protein mass in green leaves, thus interfering with proteomics studies such as LC-MS/MS and 2D-gel electrophoresis. To meet the needs for specifically and effectively separating RuBisCO from other plant proteins, Sigma developed a novel immunoaffinity matrix based on the IgY antibodies cross-linked to microbeads, which specifically removes RuBisCO protein from plant extract.

Application

Seppro® Rubisco, LC2 (2mL columns) may be used in plant proteomics research to effect IgY-mediated immune affinity removal of RuBisCO (Ribulose-1,5-bisphosphate carboxylase/oxygenase) from plant tissue extracts via liquid chromatography.

Legal Information

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

Kit Components Also Available Separately

Product No.
Description
SDS

  • S4199Seppro® Dilution bufferSDS

  • S4324Seppro® Stripping BufferSDS

  • S4449Seppro® Neutralization BufferSDS

  • CLS8163Corning® Costar® Spin-X® centrifuge tube filters, cellulose acetate membrane, pore size 0.45 μm, non-sterileSDS

Storage Class

10 - Combustible liquids


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Renato Millioni et al.
PloS one, 6(5), e19603-e19603 (2011-05-17)
To date, the complexity of the plasma proteome exceeds the analytical capacity of conventional approaches to isolate lower abundance proteins that may prove to be informative biomarkers. Only complex multistep separation strategies have been able to detect a substantial number

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