HemogloBind™ Hemoglobin Depletion From Hemolyzed Serum/Plasma

HemogloBind™ Hemoglobin Removal and Capture

  • Has a high degree of specificity for hemoglobin up to 10 mg/ml
  • Suitable for use with surfactants, chaotropes, water-soluble analytes
  • Distinquishes between hemoglobin variants
  • Applications in blood substitutes, enzyme recovery and analytical interferences

HemogloBind™ comes from a class of solid-phase, or surface-based, elastomeric poly-electrolytic surfaces that bind proteins through an empirically derived chemistry combining elements of polymer composition, cross-linking architecture and charge properties. HemogloBind™ is engineered for a high degree of selectivity and does not cross react with most common serum components, making it an excellent tool in numerous applications. These include analytical protocols where optical interference is problematic, such as bilirubin analysis and bulk serum clarification. Hemoglobin variants, as in thalassemia, bind with differential affinity towards HemogloBind™. For purification and/or analysis of hemoglobin, a modest elevation in pH will facilitate desorption of hemoglobin bound to HemogloBind™

Click here to view Hemoglobind™ Product Sheet

Kyoungsook Park, Christopher D. Saudek, and Gerald W. Hart (2010) Increased Expression of β-N-Acetylglucosamindase (O-GlcNAcase) in Erythrocytes from Prediabetic and Diabetic Individuals. Diabetes. 59(7):1845-50.

Delobel J., Rubin O., Prudent M., Crettaz D., Tissot J.-D., Lion N.(2010) Biomarker Analysis of Stored Blood Products: Emphasis on Pre-Analytical IssuesInternational Journal of Molecular Sciences. 11(11):4601-4617

Alvarez-Llamas, G., de la Cuesta, F., Barderas, M. G., Darde, V. M., Zubiri, I., Caramelo, C. and Vivanco, F. (2009), A novel methodology for the analysis of membrane and cytosolic sub-proteomes of erythrocytes by 2-DE. ELECTROPHORESIS, 30: 4095–4108

Zihao Wang, Kyoungsook Park, Frank Comer1, Linda C. Hsieh-Wilson, Christopher D. Saudek, and Gerald W. Hart (2008) Site-Specific GlcNAcylation of Human Erythrocyte Proteins: Potential Biomarker(s) for Diabetes Mellitus. Diabetes 58, 309-317.<

Datta, Pradip (2008) Effect of Hemolysis, High Bilirubin, Lipemia, Paraproteins, and System Factors on Therapeutic Drug Monitoring. Handbook of Drug Monitoring Methods, 97-109.

Yuichi Miki, Tomoki Tazawa, Kazuya Hirano, Hideki Matsushima, Shoko Kumamoto, Naotaka Hamasaki, Tomohiro Yamaguchi, Masatoshi Beppu,(2007) Clearance of oxidized erythrocytes by macrophages: Involvement of caspases in the generation of clearance signal at band 3 glycoprotein, Biochemical and Biophysical Research Communications, Volume 363, Issue 1, 9 Pages 57-62 J Krupey - US Patent App. 10/180,053, 2002 Removal of extraneous substances from biological fluids containing nucleic acids and the recovery of nucleic acids

Baion, C.M. & Ali, A.C., Evaluation Of HemogloBind™ For Removal Of O-Raffinose Crosslinked Hemoglobin (Hemolink™) From Serum, poster AACC Meeting 1997.

Padilla, S., Convenient Method for Decreasing the Amount of Hemoglobin in Tissue Samples Without Affecting the Level of Cholinesterase Activity, unpublished personal correspondence, 1994.

Sarawathi,et al., Relative quantification of glycated Cu-Zn superoxide dismutase in
erythrocytes by electrospray ionization mass spectrometry
, Biochim Biophys Acta. 1999
Feb2; 1426(3):483-90.

Person, N.B., Effect Of HemogloBind™ On Interference Reduction In Bilirubin Analysis.poster Clinichem, 1995.

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