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NRicher™ Ig
Enrichment of all isotypes and subclasses of Immunoglobulins
Consumable chemically derived beads, species agnostic as they are not derived from antibodies
Enrich circulating immune complexes 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
A comprehensive analysis of the humoral immune response (the immunome) has potential to greatly impact research across numerous fields. For example, serum autoantibodies against tumor-associated antigens have recently emerged as early stage biomarkers for different types of cancers. Most autoantibody profiling work has been based on the reactivity of unbound antibodies towards antigens produced by a variety of strategies (i.e., cDNA libraries, phage display).
An alternative approach is based on the identification of Ig-bound antigens using Liquid Chromatography coupled to Mass Spectrometry (LC-MS). Such determination of antigens complexed with antibodies at a proteome scale is critical to understanding adaptive responses in the context of infection, autoimmunity, and cancer.
Human serum immunoglobulins comprise several classes IgG, IgA, IgM, IgD & IgE. IgG is the predominant human immunoglobulin class in plasma and comprises four subclasses; ~60% are IgG1, followed by ~30% IgG2, ~7% IgG3 and ~3% IgG4. To date, most of the circulating antibody complex research has been focused on IgG as the efficiency of recovering a representative pool of IgG antibodies is well established. Generally for human serum/plasma, Protein A binds with high affinity to IgG1, IgG2, and IgG4, but poorly to IgG3. Among the four IgG subtypes in mice, Protein A has the weakest affinity for IgG1 while Protein G has affinity for all four IgG subclasses. Neither Protein A or G bind particularly well towards IgA, IgM, IgD or IgE.
Nevertheless, the ability to enrich circulating immune complexes from sera or plasma from both animals and humans with high yield and without selective loss of isotypes or subclasses can provide more comprehensive profiles. NRicher™ Ig can provide such enrichment for all immunome profiling methods. For antigen reactivity profiling, elution conditions are mild (pH 9-10), and preserve functionality. For antigen identification, bound proteins can be digested on-bead, with seamless integration to LC-MS analysis.
Click Here To View NRicher™ Ig Product Sheet
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References
Toxoplasma
gondii
Swapna
LS, Stevens GC, Sardinha-Silva A, Hu LZ, Brand V, Fusca DD, et al.
(2024)
ToxoNet: A high confidence map of protein-protein interactions in
Toxoplasma gondii.
PLoS
Comput Biol 20(6): e1012208. https://doi.org/10.1371/
journal.pcbi.1012208
"NRicher™
: Family Specific Enrichment For Targeted Proteomics"
Abstract
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™.
This bead-based technology is derived from experience of over 10
years at the forefront of manufacturing beads (i.e., ionic,
hydrophobic, hydrogen bonding, aromatic, polymeric) with differential
proteome binding properties. NRicher™
consists of consumable chemically derived porous beads, and an
adaptability to bead cocktails, even with seemingly incompatible
surface features; an important distinction of porous, over non-porous
magnetic beads. NRicher™
products do not require any specialized instruments, can be processed
using a standard microfuge, with adaptability to automated liquid
handlers.
Highlights
After
NRicher , target peptides have enriched spectral signal, even as
gradient times are reduced
NRicher
sub-proteome enrichment can minimize acquisition time, collectively
improving overall throughput, cost, and productivity
Investigate
out of the Venn Diagram box. Specific target peptides that report
functional and variant regions promise actionable insights and
potential multiplex biomarkers for disease.
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