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HemoVoid™ LC-MS On-Bead For RBC Proteomics



 
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Price: $275.00


Product Code: HVB


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Description Applications Specifications
 
  • Hemoglobin voids in flow-through >95%, with <30 minute bind/wash microfuge protocol
  • Low abundance enrichment and proteolytic trypsin digestion on the same bead.
  • Consumable, cost-effective, no column regeneration or cross-contamination
  • Species agnostic; human, rat, mouse, goat, sheep, porcine and bovine sera have been tested
  • Trypsin digestion on the bead
  • Seamless workflows and unique proteolytic efficiencies
    • No in-gel digests, no solution digests, no C18 desalting, more consistent, reproducible results
    • Compatibility with quantitative label (i.e., iTRAQ) and label-free LC-MS methods

HemoVoid™ LC-MS On-Bead is an hemoglobin depletion and enzymatic proteolytic digestion reagent kit. It removes hemoglobin from serum and plasma samples while concentrating low abundance proteins on the beads. It is ideal for applications involving LC-MS discovery and targeted proteomics.

The HemoVoid™ beads are derived from a silica-based library of individual mixed-mode polymeric ligands. The library was designed to facilitate weak binding of proteins, allowing for progressive enrichment of the low abundance proteome, with specialized voiding properties empirically derived. The HemoVoid™ beads have been adapted to a protocol specifically designed for LC-MS applications whereby the low abundance proteome adsorbed to the bead is proteolytically degraded to its peptide constituents. In this way HemoVoid™ LC-MS On-Bead integrates low abundance enrichment, with Trypsin (or other suitable protease) on-bead digestion, in a simple, highly efficient and seamless workflow for LC-MS discovery and quantitative analyses.



Click here for the HemoVoid™ LC-MS On-Bead For RBC Proteomics Product Sheet
References

Human Red Blood Cells (RBC)

HemoVoid™ On Bead Digestion Application Work On RBC by Irene Granlund, Umeå University

Red Blood Cells, Plasmodium extracts

Machado, Patrícia Isabel Pires. Pyruvate kinase and glucose-6-phosphate dehydrogenase deficiencies and their association with malaria–population genetics and proteomic studies. Diss. Universidade do Porto, 2013.

Walpurgis, Katja, et al. "Effects of gamma irradiation and 15 days of subsequent ex vivo storage on the cytosolic red blood cell proteome analyzed by 2D DIGE and Orbitrap MS." PROTEOMICS-Clinical Applications (2013).

P. Falciparum Clone 3D7 Cultured In Human Erythrocytes

Lasonder E, Green JL, Camarda G, Talabani H, Holder AA, Langsley G, Alano P. The Plasmodium falciparum schizont phospho-proteome reveals extensive phosphatidylinositol and cAMP-Protein Kinase A signalling. J Proteome Research. 2012;

Red Blood Cell Lysate

Barasa, Benjamin, and Monique Slijper. "Challenges for red blood cell biomarker discovery through proteomics." Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1844.5 (2014): 1003-1010.

Lange, Philipp F., Pitter F. Huesgen, Karen Nguyen, and Christopher M. Overall. "Annotating N termini for the Human Proteome Project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome." Journal of proteome research (2014).

Katja Walpurgis, Maxie Kohler, Andreas Thomas et al. Validated hemoglobin-depletion approach for red blood cell lysate proteome analysis by means of 2D-PAGE and Orbitrap MS. Electrophoresis.2012;

Mizukawa, B., George, A., Pushkaran, S. et al. Cooperating G6PD mutations associated with severe neonatal hyperbilirubinemia and cholestasis. Pediatric Blood Cancer.2011;56: 840-842.

Sudha Neelam, David G Kakhniashvili, Stephan Wilkens et al. Functional 20S proteasomes in mature human red blood cells Experimental Biology and Medicine.2011;236:580-591