HemogloBind™ Hemoglobin Depletion From Hemolyzed Serum/Plasma
HemogloBind™ Hemoglobin Removal and Capture
- Has a high degree of specificity for hemoglobin binding up to 10 mg/ml
- Applications in blood substitutes, enzyme recovery and analytical interferences
- Removes hemoglobin from any species including human, sheep, bovine, goat, etc
- Removes hemoglobin from organs, tissues.
- Hemoglobin removal from red blood cell lysate for proteomics and biomarker drug discovery
- The flow through fractions retain their enzymatic and biological activity
- The flow through fractions is compatible with LC-MS, activity based protein profiling and proteomic studies.
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
Dried Blood Spot(DBS)/Whole Blood
Hakuna, Lovemore, et al. "A simple assay for glutathione in whole blood."Analyst (2015).
Johns, Michael, et al. "SR-135, a peroxynitrite decomposing catalyst, enhances β-cell function and survival in B6D2F1 mice fed a high fat diet."Archives of Biochemistry and Biophysics (2015).
Asleh, Rabea, et al. "Haptoglobin Genotype-dependent Differences in Macrophage Lysosomal Oxidative Injury." Journal of Biological Chemistry289.23 (2014): 16313-16325.
J Krupey - United States Patent: 10/180,053, 2002 Removal of extraneous substances from biological fluids containing nucleic acids and the recovery of nucleic acids
Red Blood Cell (RBC) - Lysates.
Kyoungsook Park, Christopher D. Saudek, and Gerald W. Hart Increased Expression of β-N-Acetylglucosamindase (O-GlcNAcase) in Erythrocytes from Prediabetic and Diabetic Individuals. Diabetes.2010;59(7):1845-50.
Barasa, Benjamin, and Monique Slijper. "Challenges for red blood cell biomarker discovery through proteomics." Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1844.5 (2014): 1003-1010
Stored Blood Products
Delobel J., Rubin O., Prudent M., Crettaz D., Tissot J.-D., Lion N.(2010) Biomarker Analysis of Stored Blood Products: Emphasis on Pre-Analytical Issues. International Journal of Molecular Sciences. 11(11):4601-4617
Red Blood Cells/Forensic Research
Danielson, Phillip B. "Isolation of Highly Specific Protein Markers for the Identification of Biological Stains: Adapting Comparative Proteomics to Forensics." (2011).
Red Blood Cells (RBC) - Blood.
Wilhelm, Christina M., et al. A comprehensive evaluation of the efficacy of leading oxime therapies in guinea pigs exposed to organophosphorus chemical warfare agents or pesticides. Toxicology and Applied Pharmacology Available online 31 October 2014. doi:10.1016/j.taap.2014.10.009 Hikosaka, Keisuke, et al. "Deficiency of Nicotinamide Mononucleotide Adenylyltransferase 3 (Nmnat3) Causes Hemolytic Anemia by Altering the Glycolytic Flow in Mature Erythrocyte"Journal of Biological Chemistry(2014): jbc-M114.
McGarry, Kevin G., et al. "Evaluation of HemogloBind™ treatment for preparation of samples for cholinesterase analysis." (2013). Advances in Bioscience and Biotechnology, 2013, 4, 1020-1023
Alvarez-Llamas, Gloria, Fernando de la Cuesta, Maria G. Barderas, Irene Zubiri, Maria Posada-Ayala, and Fernando Vivanco. "Characterization of Membrane and Cytosolic Proteins of Erythrocytes." In Vascular Proteomics, pp. 71-80. Humana Press, 2013.
Alvarez-Llamas, G., de la Cuesta, F., Barderas, M. G., Darde, V. M., Zubiri, I., Caramelo, C., Vivanco, F. A novel methodology for the analysis of membrane and cytosolic sub-proteomes of erythrocytes by 2-DE.Electrophoresis.2009;30:4095-4108
Zihao Wang, Kyoungsook Park, Frank Comer1, Linda C. Hsieh-Wilson, Christopher D. Saudek, Gerald W. Hart. Site-Specific GlcNAcylation of Human Erythrocyte Proteins: Potential Biomarker(s) for Diabetes Mellitus. Diabetes.2008;58, 309-317.
Datta, Pradip. Effect of Hemolysis, High Bilirubin, Lipemia, Paraproteins, and System Factors on Therapeutic Drug Monitoring. Handbook of Drug Monitoring Methods.2008; 97-109.
Yuichi Miki, Tomoki Tazawa, Kazuya Hirano, Hideki Matsushima, Shoko Kumamoto, Naotaka Hamasaki, Tomohiro Yamaguchi, Masatoshi Beppu. Clearance of oxidized erythrocytes by macrophages: Involvement of caspases in the generation of clearance signal at band 3 glycoprotein. Biochemical and Biophysical Research Communications.2007; 363(1):57-62
Sarawathi,et al., Relative quantification of glycated Cu-Zn superoxide dismutase in erythrocytes by electrospray ionization mass spectrometry, Biochimica et Biophysica Acta. 1999.1426(3):483-90
Person, N.B., Effect Of HemogloBind™ On Interference Reduction In Bilirubin Analysis.poster Clinichem, 1995.
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.