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NRicher™ Apo
Enrichment of Apolipoproteins
- Consumable chemically derived beads, species agnostic as they are not derived from antibodies
- Enrich Apolipoproteins from sera or plasma from both animals and humans, >90% Albumin removal
- Does not require any specialized instruments, just a standard microfuge
- Bead format suitable for automation compatibility, please inquire
- On-Bead digestion for LC-MS analysis, or optional elution for any functional, enzymatic, or immunoassay analysis
Click Here To View NRicher™ APO Product Sheet
Apolipoproteins play a key role in atherosclerotic processes. Apo E variants are under investigation in neurological disorders, and in cancer there is evidence for modulating apolipoprotein expression. Thus, profiles of circulating apolipoproteins hold promise as biomarkers for the prediction of cardiovascular disease (CVD) and other precision medicine applications. However, clinical immunoassays are not available for most apolipoproteins, and variants require special consideration. For example, the size polymorphism of Lp(a) necessitates a need for isoform-agnostic measurement. Thus, advances in the productivity and multiplexing capacity of LC-MS/MS, offer the potential for personalized profiling by simultaneous quantification of multiple apolipoproteins and their associated variants.
The NRicher™ Apo product is dedicated to Apolipoproteins to help in these investigations. Another BSG product - Cleanascite™ binds to only lipid-bound proteins, and can be used to investigate the lipid-bound vs. unbound profile. This may provide additional granularity to CVD risk assessment.
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Product
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Size
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Total serum/plasma
samples processed
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Item No.
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NRicher™ Apo
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10 Preps
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10 x (25-50) µl samples
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NAPO-10
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NRicher™ Apo
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50 Preps
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50 x (25-50) µl samples
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NAPO-50
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References
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The article states we used affinity beads (NuGel PROspector) to pre-enrich Toxoplasma gondii lysate to capture five distinct
subproteomes. [Note: NuGel PROspector beads are now part of the NRicher™ platform.]. When comparing the 5 different
subproteomes, there is clearly different selection biases amongst the 5 surface chemistries. Also, many of the proteins
observed from the NRicher™ beads, were not observed in the Ion exchange fractions demonstrating the importance of
combining different modes (ionic, hydrophobic, etc.) of separation to alter selection properties, and consequently improving
overall proteome coverage.
Wan, C., Borgeson, B., Phanse, S. et al. Panorama of ancient metazoan macromolecular complexes. Nature 525, 339–344
(2015). hXps://doi.org/10.1038/nature14877
Six different NRicher™ beads (described with an old tradename PROspector) were used as an enrichment 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 the NRicher™ surface chemistry platform can simplify complex proteomes into enriched sub-
proteomes with efficiencies suitable for deep functional proteome characterization.
Whitepaper - NRicher™: A Low Abundance Proteome Enrichment Platform With Seamless Integration of On-Bead
Digestion
The NRicher™ Advantage is described: • Consumable chemically derived NuGel™ beads, species agnostic as they are not
derived from antibodies • Does not require any specialized instruments, just a standard microfuge • Use of bead cocktails
allows for one, rather than multiple LC-MS analyses • Functionally active sub-proteomes after separations, for any orthogonal
functional, enzymatic, or immunoassay analysis https://www.biotechsupportgroup.com/v/vspfiles/templates/257/pdf/BiotechSupportGroup-NRicher-Whitepaper.pdf
NRicher : Family Specific Enrichment For Targeted Proteomics – Poster US HUPO 2024
The need for new biomarkers to support personalized healthcare, has fostered numerous proteomic innovations. Still, a
number of challenges remain. One is the preponderance of high abundance proteins and, concurrently in targeted proteomic
workflows, efficiency and consistency in quantifying target peptides from different sample cohorts. This is in part due to the
changing landscape of proteins/peptides not associated with the selected targets. A solution for both these challenges is now
available through a suite of products called NRicher . https://www.biotechsupportgroup.com/v/vspfiles/templates/257/pdf/NRicher%20poster%20small.pdf
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