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Nature Article Cites HemogloBind™ and NRicher™ for Macromolecular Complex Annotation

MONMOUTH JUNCTION, NJ, February 9, 2016 -- Biotech Support Group reports on a recent research article published in Nature, describing the simplicity and efficiency of their proteomic enrichment technology to observe and annotate soluble multiprotein complexes common to metazoa.


The citation is:

C Wan, B Borgeson, S Phanse, F Tu, K Drew, G Clark, et al. Panorama of ancient metazoan macromolecular complexes. Nature 525, 339–344 (17 September 2015).

doi:10.1038/nature14877


In brief, the article’s authors aimed at elucidating the components of multiprotein complexes on a proteome-wide scale. The authors identify protein complexes from nine species in parallel, based on biochemical fractionation of native soluble macromolecular complexes followed by tandem mass spectrometry to identify components. The article states “…clarified heart and liver homogenates were frozen, and subsequently pooled, depleted of hemoglobin using HemogloBind™ according to manufacturer’s instructions…prior to sucrose gradient fractionation. A second Biotech Support Group product, formerly called SeraFILE PROspector and now trademarked as NRicher™ 6, was used for sub-proteome enrichment. The article states “Affinity bead based sample pre-separations were performed forC. elegans lysates as per manufacturer’s instructions…fractions (SeraFILE bead eluates) were subjected to ion exchange fractionation…”. The authors conclude that many complexes are conserved across species, and by correlating the results with genome sequence information, are able to predict more than one million interactions in 122 eukaryotes.

“I am very pleased that two of our products were able to contribute to this rigorous examination of protein complexes. When our products were used as a pretreatment step in the overall workflow, about twice the number of observations and annotations became possible. This further validates that the sub-proteome bias characteristics of NRicher™ 6 can simplify complex proteomes into less complex sub-proteomes with efficiencies suitable for deep functional proteome characterization. Furthermore, this study demonstrated the importance of a key feature implicit to all of our products; that is the maintenance of functional and structural integrity after separations. Without that particular feature, these additional observations would not have been possible.” states Swapan Roy, Ph.D., President and Founder of Biotech Support Group.