HemoVoid™ - Hemoglobin Depletion From Erythrocytes
HemoVoid™ - Hemoglobin Depletion Reagent Kit
- Hemoglobin voids in flow-through >98%, with <30 minute bind/wash/elute protocol
- Hemoglobin removal from red cell lysates for RBC proteomics
- Hemoglobin removal from hemolyzed serum, blood and dried blood spot/blood card
- Enrichment of hemoglobin variants.
- Low abundance protein and enzyme enrichment
- Disposable, cost-effective and high-throughput
- Mild elution maintains tertiary structure and simple transfer to secondary analysis
- Removes hemoglobin from species including human, sheep, bovine, goat, etc.
- Removes hemoglobin from organs, tissues.
- The eluted fractions retain their enzymatic and biological activity
- The eluted fraction is compatible with LC-MS, activity based protein profiling and proteomic studies.
HemoVoid™ , a silica-based protein enrichment matrix, removes hemoglobin from erythrocyte lysate samples while concentrating low abundance, and/or low molecular weight proteins. The HemoVoid™ protocol uses mild buffers; the protocol conditions are so gentle that native enzyme activity is retained in elution fractions.
HemoVoid™ derives from a silica-based library of individual mixed-mode ligand combinations (ionic, hydrophobic, aromatic, polymer). The library was designed to facilitate weak binding of proteins, allowing for rapid elution from the matrix without any foreknowledge of the variety of proteins contained in the starting sample. HemoVoid™ depletes hemoglobin from red cell lysates while improving the resolution of less abundant blood proteins.
For more information on HemoVoid™ HVK-100 100 Preps, 300µL of samples can be processed per prep, please contact us
Click here to view HemoVoid™ Product Sheet
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
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
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