Thermo Fisher Scientific and Intrinsic Bioprobes have announced an alliance to co-develop and market a mass spectrometric immunoassay (MSIA) workflow for research laboratories.
The alliance will focus on creating a mass spectrometry solution that will enable researchers to perform quantitative, high-throughput, high-resolution protein biomarker assays.
It is said to couple the specificity of immuno-enrichment with the sensitivity and quantitative capability of mass spectrometry to provide researchers with a more complete, higher-resolution view of the proteome.
Initially, via an exclusive reseller agreement, the solution will be applied to the detection of human parathyroid hormone (PTH) and its variants, which may be useful as biomarkers for bone diseases and diseases of the endocrine system.
As part of the arrangement, Thermo Fisher Scientific will integrate Intrinsic Bioprobes's proprietary immuno-enrichment technology with Thermo Scientific automated sample handling and mass spectrometer systems.
Scientists at the Biomarkers Initiatives in Mass Spectrometry Center will collaborate with Intrinsic Bioprobes to develop a mass spectrometric immunoassay workflow for research laboratories.
Thermo Fisher Scientific will market, distribute and support the solution and the workflow.
IBI's immuno-enrichment technology is based on the company's patented pipette tip that integrates a high-throughput, high-binding-capacity microcolumn activated with antibodies.
This technology addresses one of the key challenges of biomarker discovery and validation - the isolation and analysis of very low-abundance proteins such as PTH in complex biological matrices.
Conventional approaches involving depletion of interfering high-abundance proteins are time-consuming and introduce analytical variability.
Compared with other immuno-enrichment approaches, Intrinsic Bioprobes's approach is said to offer more effective capture of low-abundance proteins.
A key challenge in proteomics research is the ability to differentiate between, and accurately quantitate, intact proteins and their variants.
Traditional enzyme-linked immunosorbent assays (Elisa) are limited by the inability of the antibodies to discriminate between all variants and quantify their abundance.
A solution is to use the specificity of mass spectrometry to identify and quantitate microheterogeniety.
However, many researchers have been stymied by the lack of an integrated, high-throughput mass spectrometry workflow that is robust and reproducible from laboratory to laboratory.
