New Hemoglobin Capture Reagent From Blood and Hemolyzed Serum with NuGel™ Matrix

MONMOUTH JUNCTION, NJ- Biotech Support Group LLC has developed a new product for it’s line of NuGel™ affinity support and HemogloBind™ hemoglobin capture/depletion products. NuGel-HemogloBind™ is a hemoglobin capture reagent from blood and hemolyzed serum with NuGel™ matrix. NuGel-Hemoglobind™ is reengineered for increased stability. It is based on Hemoglobind™ ligand attached to NuGel™ silica covalently bound to elastomeric polyelectrolytes. Research by authors Blank et al cites how hemoglobin interfered with analyte detection of albumin, aspartate aminotransferase, direct bilirubin, total protein on the SMAC and creatinine. Intravascular hemolysis causing increased hemoglobin affects laboratory values. NuGel-Hemoglobind™ binds >95% of hemoglobin from blood and removes hemoglobin from any species including human, mouse, rat, sheep, bovine, goat etc. It also removes hemoglobin from organs and tissues. The flow through fractions(hemoglobin depleted) retain their enzymatic and biological activity. Compatible with LC-MS, activity-probe profiling and for proteomic analysis NuGel-Hemoglobind™ is developed specifically for hemoglobin removal from whole blood and hemolyzed serum for biomarker and drug discovery. It is supplied as a dry power which increases it’s shelf life and stability. The protocol is rapid, linearly scaleable up or down and is compatible with high throughput automation. NuGel-Hemoglobind™ product works similar to Hemoglobind™.

For more information, visit:
http://www.biotechsupportgroup.com/node/357

About Biotech Support Group LLC

Biotech Support Group LLC is a leading provider of proteomics and genomics sample preparation products and enrichment reagent kits as well as integrated biotechnology services for life sciences research, biomarker and drug discovery. Its principal products include: AlbuSorb™ for albumin depletion, AlbuVoid™ for albumin depletion plus low abundance serum protein enrichment, Cleanascite™ for lipid adsorption and clarification, NuGel™ for passivated silica-based affinity chromatography, ProCipitate™ & ProPrep™ for nucleic acid isolation, and for depletion and purifying hemoglobin; HemoVoid™ for depletion from red blood cells and HemogloBind™ primarily for hemolyzed serum. Biotech Support Group LLC and ProFACT Proteomics Inc., are collaborating on the development of a functional proteomics separations platform used in biomarker and functional proteomic prospecting. For more information, go to: http://www.biotechsupportgroup.com

CONTACT:

Dr. Swapan Roy & Matthew Kuruc
Biotech Support Group
1 Deer Park Drive, Suite M,
Monmouth Junction, NJ 08852, USA
732-274-2866
sales@biotechsupportgroup.com
http://www.biotechsupportgroup.com

Suggested References
Blank, DavidW, M. H. Kroll, M. E. Ruddel, and R. J. Elin. “Hemoglobin interference from in vivo hemolysis.” Clinical chemistry 31, no. 9 (1985): 1566-1569.

Lippi, Giuseppe, Martina Montagnana, Gian Luca Salvagno, and Gian Cesare Guidi. “Interference of blood cell lysis on routine coagulation testing.” (2009).
Weykamp, Cas W., Kor Miedema, Tjeerd De Haan, and Cees JA Doelman. “Carbamylated hemoglobin interference in glycohemoglobin assays.” Clinical chemistry 45, no. 3 (1999): 438-439.

Arakaki, Lorilee SL, and David H. Burns. “Multispectral analysis for quantitative measurements of myoglobin oxygen fractional saturation in the presence of hemoglobin interference.” Applied Spectroscopy 46, no. 12 (1992): 1919-1928.

Ali, Arlene CY, and Janet A. Campbell. “Interference of o-raffinose cross-linked hemoglobin with routine Hitachi 717 assays.” Clinical chemistry 43, no. 9 (1997): 1794-1796.

Lo, Stanley F., Bernadine Jendrzejczak, and Basil T. Doumas. “Total or neonatal bilirubin assays in the Vitros 5, 1 FS: hemoglobin interference, hemolysis, icterus index.” Clinical chemistry 53, no. 4 (2007): 799-800.

Simoni, Jan, Grace Simoni, Charles D. Lox, Samuel D. Prien, and G. Tom Shires. “Hemoglobin interference with an enzyme-linked immunosorbent assay for the detection of tumor necrosis factor-alpha.” Analytica chimica acta 313, no. 1 (1995): 1-14.

Algeciras-Schimnich, Alicia, Walter J. Cook, Thomas C. Milz, Amy K. Saenger, and Brad S. Karon. “Evaluation of hemoglobin interference in capillary heel-stick samples collected for determination of neonatal bilirubin.” Clinical biochemistry 40, no. 16 (2007): 1311-1316.

Schenkman, Kenneth A., and David H. Burns. “Measurement of myoglobin oxygen saturation in the presence of hemoglobin interference by near-infrared spectroscopy.” Society of Photooptical Instrumentation Engineers Proceedings 2131 (1994): 468-474.

Porter, William H., James R. Carroll, and Robert E. Roberts. “Hemoglobin interference with Du Pont Automatic Clinical Analyzer procedure for calcium.” Clinical Chemistry 23, no. 11 (1977): 2145-2147

Weykamp, C. W., T. J. Penders, C. W. Siebelder, F. A. Muskiet, and W. Van der Slik. “Interference of carbamylated and acetylated hemoglobins in assays of glycohemoglobin by HPLC, electrophoresis, affinity chromatography, and enzyme immunoassay.” Clinical chemistry 39, no. 1 (1993): 138-142.

Related HemogloBind™ References

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

Red Cell 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.

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
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

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

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

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