Press Release

HemogloBind^TM Advances Proteomic Study of Hemolytic Anemia

MONMOUTH JUNCTION, NJ, January 5, 2026 - A research pre-print entitled Ubiquitination and degradation of CD47 enhances macrophage phagocytosis of hemolytic erythrocytes, describes HemogloBind^TM methods to advantage in a proteomic comparison of erythrocytes.

A form of hemolytic anemia, classical complement pathway-mediated hemolysis involves the immune system's destruction of red blood cells (RBCs). However, the mechanisms involved in clearing RBC membrane remnants remain to be elucidated. A self marker on RBCs, CD47, is essential for erythrophagocytosis, interacting with signal regulatory protein alpha (SIRP-alpha) to transmit a do not eat me signal to macrophages. To study the mechanism underlying the reduced expression of CD47, a mass spectrometry-based proteomic analysis of both hemolytic and normal RBCs was performed, leading to the identification of 1040 proteins.

The use of HemogloBind^TM was essential to the proteomic comparison, functional annotation and biological significance of these proteins, as their differential expressions offered valuable insights into the mechanism of CD47 downregulation. Collectively, the enrichment data from their functions and pathways pointed to a possible link between CD47 degradation and the ubiquitin-proteasome-system (UPS). Therefore, the proteomic findings offered a foundation for proposing and testing a hypothesis that ubiquitination could be a principal mechanism responsible for the reduced levels of CD47 in erythrocytes during the hemolytic process.

The study concludes that a significant downregulation of CD47 is observed on the membranes of erythrocyte ghosts due to ubiquitin-proteasome-mediated degradation, facilitating their phagocytic removal by macrophages. These findings uncover a critical pathway for the efficient clearance of hemolytic remnants, offers alternative perspectives on post-hemolytic immune homeostasis, and suggests potential therapeutic avenues for reducing complications associated with hemolysis. Swapan Roy, Ph.D., President and Founder of Biotech Support Group, states that this is an excellent example of how our Hemoglobin depletion product, HemogloBind^TM, contributed to differential proteome expression analysis of red cells, and that ultimately lead to the conclusions of this study. As Hemoglobin accounts for about 95% of the protein mass in red cell lysates, it is necessary to efficiently remove Hemoglobin and recover the vast majority of the remaining red cell proteome for LC-MS analysis.

For more information on HemogloBind^TM, visit:

HemogloBind Hemoglobin Depletion From Hemolyzed Serum/Plasma

For more information of all of our Hemoglobin removal products, visit:

Hemoglobin Removal Kits

About Biotech Support Group LLC Biotech Support Group develops innovative sample preparation technologies that address the emerging needs of proteomics, biomarker discovery, and personalized medicine. Flagship products include Cleanascite^TM for lipid removal, AlbuVoid^TM and AlbuSorb^TM PLUS for serum protein depletion, HemogloBind^TM and HemoVoid^TM for hemoglobin removal, and NRicher^TM for low abundance, family specific, and targeted proteome enrichment. These products support translational research by simplifying workflows and improving sample quality for downstream analysis.

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Matthew Kuruc Phone: 732-274-2866
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Keywords: HemogloBind^TM, Hemoglobin depletion, Hemoglobin removal, erythrocyte proteomics, hemolytic anemia