HemoVoid™ LC-MS On-Bead For RBC Proteomics
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
abundanceproteome 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
• 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
* 보다 큰 그림과 자세한 내용은 아래 Application Report의 PDF 파일 및 References의 Human Red Blood Cells의
PDF 파일을 참고하시기 바랍니다.
Dr.Roy, Matthew Kuruc, et al. "Hemoglobin Removal Reference Applications Report (PDF)
Human Red Blood Cells (RBC)
HemoVoid™ On Bead Digestion Application Work On RBC (PDF) 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