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Biotech Support Group Release: Hemoglobin Enrichment From Dried Blood Spot (DBS) for Hemoglobin Variant Research


10/15/2012 1:46:16 PM

PRLog (Press Release) - Oct 14, 2012 -- MONMOUTH JUNCTION, NJ.– HemoVoid™ Blood Card is developed specifically for the purification & enrichment of hemoglobin from blood for hemoglobin variant research. It is compatible with protocols which require direct surface sampling of dried blood spot (DBS) to identify intact proteins. Pharmaceutical testing of DBS samples from clinical matrices for bioanalytical applications during the drug development process favors DBS technology because of reduced animal consumption, reduced shipping costs, storage at ambient temperature and decreased infection risk and toxicity. With HemoVoid™ Blood Card, the enriched hemoglobin voids in flow-through greater than 98% pure, with less than 30 minute bind/wash/elute protocol. Researchers studying hemoglobin variant (HbS, HbE, HbC, HbD, HbF, HbA1c,Thalassemia, etc) should implement HemoVoid™ Blood Card’s efficient protocol. Mild buffer condition maintains tertiary structure and simple transfer to secondary analysis.

The hemoglobin enriched filtrate could have hemoglobin variants, hemoglobin binding proteins or other analytes optimal for biomarker studies. Eluted fractions contains hemoglobin depleted proteins which can be used for developing and validating LC-MS, proteomic studies including protein identification characterizing low abundance proteins for protein biomarker research and gain a broader understanding of the structural, catalytic and signaling functions of such proteins.

HemoVoid™ features an easy to implement sample preparation protocol. It is disposable, cost-effective and high-throughput compatible for the detection of the variant peptides making it an ideal choice for hemoglobin variants discovery for hemoglobin proteomics research. HemoVoid™ , a silica-based protein enrichment matrix, removes hemoglobin from erythrocyte lysate samples while concentrating low abundance, and/or low molecular weight proteins.

For more information about Hemovoid™ Blood Card, click:

http://www.biotechsupportgroup.com/node/238

About Biotech Support Group LLC

Biotech Support Group LLC is a leading provider of genomics and proteomics sample preparation products and enrichment reagent kits as well as integrated biotechnology services for life sciences research, biomarker and drug discovery. Based in New Jersey, it’s principal products include: AlbuVoid™ for albumin depletion, Cleanascite™ for lipid adsorption and clarification, NuGel™ for passivated silica-based affinity chromatography, and ProCipitate™ & ProPrep™ for nucleic acid isolation. Biotech Support Group is the leading developer of sample preparation products for separating and purifying hemoglobin from blood samples. HemoVoid™ is a hemoglobin depletion reagent kit from red blood cells and HemogloBind™ is a hemoglobin capture reagent from hemolyzed serum. Currently, Biotech Support Group LLC and ProFACT Proteomics Inc., are collaborating on the development of a proteomics platform used in functional profiling for proteomic analysis and a separations method for generating sub-proteomes used in biomarker and functional proteomic prospecting. For more information, go to: www.biotechsupportgroup.com

CONTACT:

Dr.Swapan Roy

Biotech Support Group

1 Deer Park Drive, Suite M,

Monmouth Junction, NJ 08852, USA

732-274-2866

sales@biotechsupportgroup.com

Related HemoVoid™ References

1.Lasonder E, Green JL, Camarda G, Talabani H, Holder AA, Langsley G, Alano P. The Plasmodium falciparum schizont phospho-proteome reveals extensive phosphatidylinositol and cAMP-Protein Kinase A signalling. J Proteome Research. 2012;

2.Katja Walpurgis, Maxie Kohler, Andreas Thomas et al.Validated hemoglobin-depletion approach for red blood cell lysate proteome analysis by means of 2D-PAGE and Orbitrap MS.Electrophoresis.2012;

3.Mizukawa, B., George, A., Pushkaran, S. et al. Cooperating G6PD mutations associated with severe neonatal hyperbilirubinemia and cholestasis.Pediatric Blood Cancer.2011;56: 840-842.

4.Sudha Neelam, David G Kakhniashvili, Stephan Wilkens et al. Functional 20S proteasomes in mature human red blood cells Experimental Biology and Medicine.2011;236:580-591

Suggested References:

1.Basilico, F., Di Silvestre, D., Sedini, S., Petretto, A., Levreri, I., Melioli, G., Farina, C., Mori, F. and Mauri, P. L. (2007), New approach for rapid detection of known hemoglobin variants using LC-MS/MS combined with a peptide database. J. Mass Spectrom., 42: 288–292.

2.Hardison R, Chui DHK, Riemer C, Miller W, Carver M, Molchanova T, Efremov G, and Huisman THJ (1998). Access to ``A Syllabus of Human Hemoglobin Variants (1996)'' via the World Wide Web. Hemoglobin 22: 113-127

3.Edwards RL, Creese AJ, Baumert M, Griffiths P, Bunch J, Cooper HJ. Hemoglobin variant analysis via direct surface sampling of dried blood spots coupled with high-resolution mass spectrometry. Anal Chem. 2011 Mar 15;83(6):2265-70.

4.Fishleder, AJ and Hoffman, GC. A practical approach to the detection of hemoglobinopathies: Part III. Lab Med 1987;18:513.

5.Globin Gene Server, HbVar: a database of human hemoglobin variants and Thalassemias. http://globin.cse.psu.edu/cgi-bin/hbvar/counter

6.Shimizu A, Nakanishi T, Kishikawa M, Miyazaki A.Detection and identification of protein variants and adducts in blood and tissues: an application of soft ionization mass spectrometry to clinical diagnosis.J Chromatogr B Analyt Technol Biomed Life Sci.25;776(1):15-30.

7.Edwards RL, Griffiths P, Bunch J, Cooper HJ.Top-Down Proteomics and Direct Surface Sampling of Neonatal Dried Blood Spots: Diagnosis of Unknown Hemoglobin Variants.J Am Soc Mass Spectrom. 2012

8.Crawford E, Gordon J, Wu JT, Musselman B, Liu R, Yu S.Direct analysis in real time coupled with dried spot sampling for bioanalysis in a drug-discovery setting.Bioanalysis. 2011 Jun;3(11):1217-26.

9.Spooner N, Lad R, Barfield MDried blood spots as a sample collection technique for the determination of pharmacokinetics in clinical studies: considerations for the validation of a quantitative bioanalytical method. Anal Chem. 2009 Feb 15;81(4):1557-63.

10.Witkowska HE, Bitsch F, Shackleton CH.Expediting rare variant hemoglobin characterization by combined HPLC/electrospray mass spectrometry.Hemoglobin. 1993 Jun;17(3):227-42.

11.Shackleton CH, Falick AM, Green BN, Witkowska HE.Electrospray mass spectrometry in the clinical diagnosis of variant hemoglobins.J Chromatogr. 1991 Jan 2;562(1-2):175-90.

12.Rahbar S, Lee TD, Baker JA, Rabinowitz LT, Asmerom Y, Legesse K, Ranney HM.

13.Reverse phase high-performance liquid chromatography and secondary ion mass spectrometry. A strategy for identification of ten human hemoglobin variants.Hemoglobin. 1986;10(4):379-400.

14.Falick AM, Shackleton CH, Green BN, Witkowska HE.Tandem mass spectrometry in the clinical analysis of variant hemoglobins.Rapid Commun Mass Spectrom. 1990 Oct;4(10):396-400.

15.Witkowska HE, Bitsch F, Shackleton CH.Expediting rare variant hemoglobin characterization by combined HPLC/electrospray mass spectrometry.Hemoglobin. 1993 Jun;17(3):227-42.

16.Williams JP, Giles K, Green BN, Scrivens JH, Bateman RHIon mobility augments the utility of mass spectrometry in the identification of human hemoglobin variants.Rapid Commun Mass Spectrom. 2008 Oct;22(20):3179-86.

17.Pucci P, Carestia C, Fioretti G, Mastrobuoni AM, Pagano L. Protein fingerprint by fast atom bombardment mass spectrometry: characterization of normal and variant human haemoglobins.Biochem Biophys Res Commun. 1985 Jul 16;130(1):84-90.

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