MONMOUTH JUNCTION, NJ.– Biotech Support Group, LLC has been researching and creating innovative genomic and proteomic products for over 15 years. One of the new breakthroughs in our protein purification research is the novel method of separating and purifying hemoglobin from blood samples. Clinical researchers as well as lab technicians have been using Biotech Support Group’s HemoVoid™ in various different applications in order to separate hemoglobin itself, from a milieu of proteins, in order to study the various antibodies, and biomarkers located on hemoglobin’s surface. This is possible because hemoglobin retains its tertiary structure, and is not being denatured nor destroyed in the separation process.

Researchers using HemoVoid™ can study purified hemoglobin from a blood sample, or choose to study the other blood proteins, without the interference of hemoglobin.

HemoVoid™ will allow researchers and scientists to understand how hemoglobin itself works. Through the science discovered at Biotech Support Group, HemoVoid™ remains one of the only products in the market today that can separate hemoglobin from a blood sample, without destroying the intrinsic bonds within the protein.

A NEW HemoVoid™ Application: Hemoglobin Enrichment Protocol From Blood Sample For Hemoglobin Variant Research (HbS, HbF, HbA, HbA1c, Thalassemia, etc.)

• Enriched Hemoglobin voids in flow-through >98% pure, with <30 minute bind/wash/elute protocol
• Hemoglobin Enrichment from Whole Blood, RBC Lysate, and Blood Card
• Disposable, cost-effective
• Mild elution maintains tertiary structure and simple transfer to secondary analysis
• Enriches hemoglobin from diverse species inc. human, sheep, mouse, goat, rat, etc.
• Eluted fractions contains Hemoglobin depleted proteins which can be used for proteomic studies

Quantification and subsequent analysis of the Hb fractions and variants is possible by implementing combination of cation-exchange high performance chromatography (CE-HPLC), capillary electrophoresis (CE) and when possible isoelectric focusing (IEF). The HemoVoid™ reagent kit is compatible with HPLC analysis of hemoglobin variants by cation exchange procedure which allows the separation of normal and numerous variant hemoglobins as dimers, or the reversed phase method making it possible to separate polypeptide chains.

For more information about HemoVoid™ protocol for hemoglobin enrichment, click here:

For more information about HemoVoid™, click here.

CONTACT:
Dr. Swapan Roy & Matthew Kuruc
Biotech Support Group LLC
1 Deer Park Drive, Suite M
Monmouth Junction NJ 08852
732-274-2866 Worldwide
800-935-0628 North America
sales@biotechsupportgroup.com
http://www.biotechsupportgroup.com

HemoVoid™ References:

1. Mizukawa, B., George, A., Pushkaran, S., Weckbach, L., Kalinyak, K., Heubi, J. E. and Kalfa, T. A. , Cooperating G6PD mutations associated with severe neonatal hyperbilirubinemia and cholestasis. Pediatric Blood & Cancer.
2. Functional 20S proteasomes in mature human red blood cells Sudha Neelam, David G Kakhniashvili, Stephan Wilkens,Stephen D Levene and Steven R Goodman Exp. Biol. Med. 2011;236:580-591 doi:10.1258/ebm.2011.010394

Suggested References:

1. Hardison RC, Chui DHK, Giardine B, Riemer C, Patrinos GP, Anagnou N, et al. HbVar: a relational database of human hemoglobin variants and thalassemia mutations at the globin gene server. Hum Mut 2002;19:225-233.
2. Wajcman H, Préhu C, Bardakdjian-Michau J, Promé D, Riou J, Godart C, et al. Abnormal hemoglobins: laboratory methods. Hemoglobin. 2001;25:169–81
3. Clarke G, Higgins TN. Laboratory investigation of hemoglobinopathies and thalassemia: review and update. Clin Chem 2000;46:1284-1290
4. Riou J, Godart C, Hurtrel D, Mathis M, Bimet C, Bardakdjian-Michau J, et al. Cation-exchange HPLC evaluated for presumptive identification of haemoglobin variants. Clin Chem. 1997;43:34–9
5. Ou C-N, Rogerud CL. Rapid analysis of hemoglobin variants by cation-exchange HPLC. Clin Chem 1993;39:820-824

For this new application protocol, please contact us by phone or email.