PressRelease
HemogloBind™Advances Proteomic Study of Hemolytic Anemia
MONMOUTHJUNCTION, NJ, January 5, 2026–Aresearch pre-print entitled “Ubiquitinationand degradation of CD47 enhances macrophage phagocytosis of hemolyticerythrocytes“,describes HemogloBind™methods to advantage in a proteomic comparison of erythrocytes.
Aform of hemolytic anemia, classical complement pathway-mediatedhemolysis involves the immune system’s destruction of red bloodcells (RBCs). However, the mechanisms involved in clearing RBCmembrane remnants remain to be elucidated. A “self” marker onRBCs, CD47, is essential for erythrophagocytosis, interacting withsignal regulatory protein alpha (SIRPα) to transmit a “don’t eatme” signal to macrophages. To study the mechanism underlying thereduced expression of CD47, a mass spectrometry-based proteomicanalysis of both hemolytic and normal RBCs was performed, leading tothe identification of 1040 proteins.
Theuse of HemogloBind™ wasessential to the proteomic comparison, functional annotation andbiological significance of these proteins, as their differentialexpressions offered valuable insights into the mechanism of CD47downregulation. Collectively, the enrichment data from theirfunctions and pathways pointed to a possible link between CD47degradation and the ubiquitin-proteasome-system (UPS). Therefore, theproteomic findings offered a foundation for proposing and testing ahypothesis that ubiquitination could be a principal mechanismresponsible for the reduced levels of CD47 in erythrocytes during thehemolytic process.
Thestudy concludes that a significant downregulation of CD47, isobserved on the membranes of erythrocyte ghosts due toubiquitin-proteasome-mediated degradation, facilitating theirphagocytic removal by macrophages. These findings uncover a criticalpathway for the efficient clearance of hemolytic remnants, offersalternative perspectives on post-hemolytic immune homeostasis, andsuggests potential therapeutic avenues for reducing complicationsassociated with hemolysis.
“This is anexcellent example of how our Hemoglobin depletion product,HemogloBind™, contributed to differential proteome expressionanalysis of red cells, and that ultimately lead to the conclusions ofthis study.As Hemoglobin accounts for about95% of the protein mass in red cell lysates, it is necessary toefficiently remove Hemoglobin and recover the vast majority of theremaining red cell proteome for LC-MS analysis.”states Swapan Roy, Ph.D.,President and Founder of Biotech Support Group.
Formore information on HemogloBind™, visit:
https://www.biotechsupportgroup.com/HemogloBind-Hemoglobin-Depletion-From-Hemolyzed-p/h0145.htm
Formore information of all of our Hemoglobin removal products, visit:
https://www.biotechsupportgroup.com/Hemoglobin-Removal-s/312.htm
AboutBiotech Support Group LLC
BiotechSupport Group develops innovative sample preparation technologiesthat address the emerging needs of proteomics, biomarker discovery,and personalized medicine. Flagship products include Cleanascite™for lipid removal, AlbuVoid™ and AlbuSorb™ PLUS for serum proteindepletion, HemogloBind™ and HemoVoid™ for hemoglobin removal,and NRicher™ for low abundance, family specific, and targetedproteome enrichment.These products support translational research by simplifyingworkflows and improving sample quality for downstream analysis.
ForBusiness Development Inquiries:
Matthew Kuruc
Phone:732-274-2866
Email: [email protected]
Keywords:HemogloBind™, Hemoglobin depletion, Hemoglobin removal, erythrocyteproteomics, hemolytic anemia