Research Articles Cites HemogloBind™ in Proteomic Analysis of Red Blood Cells
Biotech Support Group reports on a journal article describing the simplicity and efficiency of HemogloBind™, to remove Hemoglobin prior to LC-MS/MS proteomic analysis.

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Research Articles Cites HemogloBind™ in Proteomic Analysis of Red Blood Cells


MONMOUTH JUNCTION, NJ, April 21, 2025 -- Biotech Support Group reports on a journal article describing the simplicity and efficiency of HemogloBind™, to remove Hemoglobin prior to LC-MS/MS proteomic analysis.

Research Articles Cites HemogloBind™ in Proteomic Analysis of Red Blood Cells Chen, Yaozhen, et al. "Red blood cells undergo lytic programmed cell death involving NLRP3." Cell (2025).


The canonical complement-mediated lysis of mature red blood cells (RBCs) leads to severe pathogenesis. However, inhibition strategies targeting complement are not always as efficient as expected. In this study, the intracellular events in mature RBCs following complement activation were investigated. The collected evidence demonstrates that complement induced hemolysis is a caspase-8-dependent programmed RBC death. To study the downstream signaling of activated caspase-8 in mature RBCs, the authors conducted a label-free proteomic analysis. For this, the article states “Mass-spectrometric analysis of differentially expressed proteins in complement-activated RBCs Human RBC lysates (from both control and complement-treated groups) were prepared asResearch Articles Cites HemogloBind™ in Proteomic Analysis of Red Blood Cells described previously. Hemoglobin was depleted by adding 250 µl of HemogloBind suspension (Biotech Support Group, Catalog #HO145-05) to each lysate. …the hemoglobin-depleted supernatant…was then subjected to liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis”. The results compare complement activation in RBCs with the control group (Figure 4A). Gene Ontology (GO) analysis revealed significant enrichment of pathways associated with cytoskeleton organization and actin filament assembly dynamics (Figure 4B). The study concludes that activated caspase-8 directly induces the proteolysis of β-spectrin, thereby disrupting the skeletal network of the RBC membrane, a process referred to as spectosis. Spectosis signaling is also activated in autoimmune hemolytic anemia or paroxysmal nocturnal hemoglobinuria, and the inhibition of spectosis significantly reduced complement-induced hemolysis. These findings reveal a programmed death cascade in mature RBCs, which may have important implications for the treatment of hemolytic disorders.


Hemoglobin accounts for about 95% of the protein mass in red cells. So for proteomics, it is necessary to efficiently remove Hemoglobin but still recover the vast majority of the remaining red cell proteome for LC-MS analysis. This is an excellent example of how our Hemoglobin depletion product, HemogloBind™, contributed to differential proteome analysis of red cells, and that ultimately lead to the conclusions of this study.states Swapan Roy, Ph.D., President and Founder of Biotech Support Group.

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Keywords: Hemoglobin depletion, HemogloBind™, LC-MS/MS, red cell proteomics, programmed cell death, caspase-8, hemolytic disorders, autoimmune hemolytic anemia, paroxysmal nocturnal hemoglobinuria


About Biotech Support Group LLC

Converging with cultural and technological disruptions forthcoming in healthcare, Biotech Support Group develops methods for cost effective and efficient sample prep essential for expanding proteomic analysis. Following a tiered business strategy, the company continues its growth in the consumable research products area. For this market, key products include: AlbuVoid™ and AlbuSorb™ PLUS for albumin & IgG depletion, Cleanascite™ for lipid adsorption, HemogloBind™ and HemoVoid™ for hemoglobin removal, and NRicher™ for low abundance and family specific, and targeted proteome enrichment. For more information, go to http://www.biotechsupportgroup.com


For business development contact: Matthew Kuruc
732-274-2866 mkuruc@biotechsupportgroup.com