Press Release

HemogloBind™ 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™ 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 (SIRPα) to transmit a “don’t 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™ 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.

“This is an excellent example of how our Hemoglobin depletion product, HemogloBind™, 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.” states Swapan Roy, Ph.D., President and Founder of Biotech Support Group.

For more information on HemogloBind™, visit:

https://www.biotechsupportgroup.com/HemogloBind-Hemoglobin-Depletion-From-Hemolyzed-p/h0145.htm

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

https://www.biotechsupportgroup.com/Hemoglobin-Removal-s/312.htm

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™ for lipid removal, AlbuVoid™ and AlbuSorb™ PLUS for serum protein depletion, HemogloBind™ and HemoVoid™ for hemoglobin removal, and NRicher™ for low abundance, family specific, and targeted proteome enrichment. These products support translational research by simplifying workflows and improving sample quality for downstream analysis.

For Business Development Inquiries:
Matthew Kuruc
Phone: 732-274-2866
Email: [email protected]

Keywords: HemogloBind™, Hemoglobin depletion, Hemoglobin removal, erythrocyte proteomics, hemolytic anemia