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HemogloBind™ Trial Kit - 5 ml Hemoglobind™ & 5 Preps of NuGel-HemogloBind™

HemogloBindâ„¢ Trial Kit - 5 ml Hemoglobindâ„¢ & 5 Preps of NuGel-HemogloBindâ„¢


Base Price: $365.00

Product Code: HB145K


HemogloBind™ was derived from a family of acid-alcohol elastomeric co-polymers. These polymers are synthesized to have separation characteristics like salts and solvents, but with the mechanical advantages: simple removal of the bound macromolecules with no solute carryover, and adaptability to filtration, centrifugation, and automation. 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™.

Characteristics of 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 are compatible with LC-MS, activity based protein profiling and proteomic research.
NuGel™ HemogloBind™ has similar separations performance but is supplied as a dry powder, rather than as a liquid suspension. NuGel-Hemoglobind™ is reengineered for increased stability. It is based on NuGel™ silica (50 microns in size, 1000Å) covalently bound to elastomeric polyelectrolytes. It binds >95% of hemoglobin from blood.
Characteristics of NuGel-Hemoglobind™ - Hemoglobin Capture Reagent From Blood and Hemolyzed Serum with NuGel™ Matrix
  • Has a high degree of specificity for hemoglobin binding up to 10 mg/ml
  • Removes hemoglobin from any species including human, mouse, rat, 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(hemoglobin depleted) retain their enzymatic and biological activity
  • The flow through fractions(hemoglobin depleted) is compatible with LC-MS, activity based protein profiling and proteomic studies.
  • Linearly scaleable up or down. Easy high throughput automation.
Click Here For The NuGel-Hemoglobind™ Product Sheet
Click Here For The HemogloBind™ Product Sheet
Click Here For The HemogloBind™ Hemoglobin Depletion Performance On Blood Sheet


HemogloBind™ References

Cell Lines

Wan, Cuihong, et al. "
Proteome-wide dataset supporting the study of ancient metazoan macromolecular complexes." Data in Brief (2015).

Dried Blood Spot(DBS)/Whole Blood

Hakuna, Lovemore, et al. " A simple assay for glutathione in whole blood."Analyst (2015).

Whole Blood

Parvathi S. Kumar, Haree K. Pallera, Pamela S. Hair, Magdielis Gregory Rivera, T
ushar A. Shah, Alice L. Werner,Frank A. Lattanzio, Kenji M. Cunnion, and Neel K. Krishna. Peptide inhibitor of complement C1 modulates acute intravascular hemolysis of mismatched red blood cells in rats.TRANSFUSION Volume 00, May 2016. doi:10.1111/trf.13674

Snider, Thomas H., Christina M. Wilhelm, Michael C. Babin, Gennady E. Platoff Jr, and David T. Yeung. "Assessing the therapeutic efficacy of oxime therapies against percutaneous organophosphorus pesticide and nerve agent challenges in the Hartley guinea pig."The Journal of Toxicological Sciences 40, no. 6 (2015): 759-775.

Brittain, Matthew K., Kevin G. McGarry, Robert A. Moyer, Michael C. Babin, David A. Jett, Gennady E. Platoff, and David T. Yeung et al. "Efficacy of Recommended Prehospital Human Equivalent Doses of Atropine and Pralidoxime Against the Toxic Effects of Carbamate Poisoning in the Hartley Guinea Pig." International journal of toxicology (2016): 1091581816638086.

Blood Plasma

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.

Biological Fluids

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

Lung Tissue Specimens & Pulmonary Research (Acute Respiratory Distress Syndrome & Acute Hypoxic Failure)

Bhargava, Maneesh"
"Proteomic Studies in Acute Hypoxic Respiratory Failure." PhD diss., UNIVERSITY OF MINNESOTA. (2015).

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.