Products

HemoVoid™ - Blood Card Reagent

Hemoglobin Depletion Plus Protein Enrichment From Blood Card 

Hemoglobin is a common contaminant from whole blood. The HemoVoid™ Blood Card protocol was

designed to substantially reduce the presence of hemoglobin and its associated interference with many

serum protein analytes. HemoVoid™ Blood Card is a silica based polyelectrolyte matrix, removes

hemoglobin from dried whole blood card samples.  The HemoVoid™ protocol uses mild buffers; the protocol

conditions areso gentle that native enzyme activity is retained in elution fractions. 

Features

• Hemoglobin voids in flow-through >98%, with <30 minute bind/wash/elute protocol

• Hemoglobin removal from whole blood lysates extracted from dried blood cards  

• Hemoglobin removal from frozen and fresh whole blood

• Blood proteins and enzymes are enriched for potential biomarker and proteomic studies.

• Disposable, cost-effective hemoglobin depletion sample preparation protocol

• Removes hemoglobin from whole blood of diverse species including human, mice, sheep, bovine,

  goat, rat, etc. 

Hemovoid Blood Card Research Applications

The HemoVoid™ Blood Card produces enriched proteins free of hemoglobin which are used for biomarkers

and protein analysis(B). The hemoglobin enriched filtrate could have hemoglobin variants, hemoglobin

binding proteins or other analytes optimal for biomarker studies(A). 

그림

Abs at 410 nm shows presence of hemoglobin.

Proteins extracted from dried blood card show high hemoglobin concentration.

After HemoVoid™ treatment, hemoglobin is severely depleted.

References

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