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Start your RBC proteome research with HemoVoid™ from Biotech Support Group MONMOUTH JUNCTION, N.J. — HemoVoid™, removes hemoglobin from erythrocyte lysate samples allowing for subsequent detection, identification and quantification of depleted hemoglobin samples The challenge in proteome analysis is overcoming the interference by high-abundance proteins obscuring less-abundant proteins.Promising new pathways in hemoglobin research begin to appear as novel molecular diagnostic technology from Biotech Support Group transforms drug discovery by allowing hemoglobin removal from red cell lysates and hemolyzed serum or plasma.Detailed human erythrocyte proteome studies are severely hampered by the presence of hemoglobin, which accounts for more than 98% of the total erythrocyte soluble protein content. HemoVoid™ from Biotech Support Group, is developed with a specific depletion approach that resulted in a drastic increase in the number of identified proteins. This depletion technique may be valuable for proteome studies of human erythrocyte disorders with unknown etiology and of tissue samples that contain blood. A new article published in the Society for Experimental Biology and Medicine journal cites HemoVoid™ Functional 20S proteasomes in mature human red blood cells The purpose of the present study was to investigate whether functional 20S and/or 26S proteasomes are present within mature human red blood cells (RBCs; depleted of reticulocytes and leukocytes). Double-immunofluorescence confocal microscopy showed the presence of immunoreactive 20S and 19S proteasomal subunit proteins and their partial co-localization within mature RBCs. Proteasomes isolated from mature RBCs displayed 20S activity in vitro; atomic-force and transmission electron microscopy of isolated proteasomes revealed abundant 20S core particles and very few 26S particles. A two-dimensional differential in-gel electrophoresis (2D-DIGE) approach was used to determine if proteasome-dependent protein degradation occurs within mature RBCs. Twenty-eight proteins were identified with altered protein content in response to lactacystin. Seven cytosolic proteins showed an increase and 16 showed a decrease; five membrane proteins showed a decrease. We conclude that the proteins showing increased abundance are either primary or secondary targets of the 20S proteasome and that putatively degraded proteins are secondary targets. Therefore, functional 20S proteasomes exist within mature RBCs. Our study did not detect 26S proteasome activity using the 2D-DIGE approach. Functional 20S Proteasomes in Mature Human Red Blood Cells About Biotech Support Group LLC Biotech Support Group LLC is a leading developer of proteomic and genomic sample preparation and enrichment products. Its principal products include: AlbuVoid™ for albumin depletion, Cleanascite™ for lipid adsorption and clarification, HemogloBind™ & HemoVoid™ for hemoglobin removal, NuGel™ for functional & chemical proteomics, and ProCipitate™ & ProPrep™ for nucleic acid isolation. For more information, go to www.biotechsupportgroup.com. CONTACTS:
Dr. Swapan Roy & Matthew Kuruc
Posted on Date:
Tue, 05/10/2011
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