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The Aptamarker platform’s capacity to apply the same 16.8 million sequences to various samples, including biological fluids, cells, or tissue on slides, represents a powerful tool for identifying variation in protein abundance across different phenotypes. This can be done with a single Next-Generation Sequencing (NGS) analysis to characterize all aptamer-target complexes.
The Aptamarker platform can achieve everything that is possible with other next-generation proteomics platforms and more. The depth of our system allows for multiple Aptamarkers binding to the same protein, thus enabling direct epitope mapping. By enabling epitope characterization, the platform extends analysis beyond canonical reference proteins to the forms of proteins actually found in vivo in a disease state. This includes complexes, isoforms, cleavage events, post-translational modifications, and foldings.
We are currently working to develop the knowledge base necessary to identify all proteins in the human proteome. This will be possible with a single Aptamarker library, and a single NGS analysis per sample.
The Aptamarker platform’s capacity to apply the same 16.8 million sequences to various samples, including biological fluids, cells, or tissue on slides, represents a powerful tool for identifying variation in protein abundance across different phenotypes. This can be done with a single Next-Generation Sequencing (NGS) analysis to characterize all aptamer-target complexes.
The Aptamarker platform can achieve everything that is possible with other next-generation proteomics platforms and more. The depth of our system allows for multiple Aptamarkers binding to the same protein, thus enabling direct epitope mapping. By enabling epitope characterization, the platform extends analysis beyond canonical reference proteins to the forms of proteins actually found in vivo in a disease state. This includes complexes, isoforms, cleavage events, post-translational modifications, and foldings.
We are currently working to develop the knowledge base necessary to identify all proteins in the human proteome. This will be possible with a single Aptamarker library, and a single NGS analysis per sample.
Aptamers are single stranded oligonucleotides that mimic antibodies in their ability to bind to target molecules. Up until now, aptamer selection has been based on SELEX, a method that implicitly requires the use of different sequences for each selection and requires immobilization of the target in order to facilitate separation of bound and unbound sequences. We have made the following proprietary innovations to enable the Aptamarker approach.
Aptamers are single stranded oligonucleotides that mimic antibodies in their ability to bind to target molecules. Up until now, aptamer selection has been based on SELEX, a method that implicitly requires the use of different sequences for each selection and requires immobilization of the target in order to facilitate separation of bound and unbound sequences. We have made the following proprietary innovations to enable the Aptamarker approach.
A library designed to maximize structural diversity while consisting of the same 16.8 million sequences.
The use of immobilized antisense as a competitor for the target to enable partitioning of bound Aptamarkers to unbound ones. This enables selection of Aptamarkers without a need to immobilize the target.
We apply the same library of sequences to different samples where the samples vary for a medical condition or propensity for a medical condition. We characterize the effect of selection on structures within this library with a single round of selection and a single NGS analysis.
We have predicted the structures of all 16.8M sequences. Discrete networks of related structures are defined in Cytoscape.Each network likely defines a different epitope on the target protein. This is the basis for the capacity to define non-canonical differences
A library designed to maximize structural diversity while consisting of the same 16.8 million sequences.
The use of immobilized antisense as a competitor for the target to enable partitioning of bound Aptamarkers to unbound ones. This enables selection of Aptamarkers without a need to immobilize the target.
The concept of working from the top down to identify Aptamarkers that bind to target molecules rather than from the bottom up, identifying one aptamer at a time. We apply the same library of sequences to different samples where the samples vary for a medical condition or propensity for a medical condition. We characterize the effect of selection on structures within this library with a single round of selection and a single NGS analysis.
We use the FRELEX concept, an immobilized competitor antisense to determine the relative proportion of a target protein being bound by an individual Aptamarker. This is then directly quantified by qPCR analysis.
A library designed to maximize structural diversity while consisting of the same 16.8 million sequences.
The use of immobilized antisense as a competitor for the target to enable partitioning of bound Aptamarkers to unbound ones. This enables selection of Aptamarkers without a need to immobilize the target.
The concept of working from the top down to identify Aptamarkers that bind to target molecules rather than from the bottom up, identifying one aptamer at a time. We apply the same library of sequences to different samples where the samples vary for a medical condition or propensity for a medical condition. We characterize the effect of selection on structures within this library with a single round of selection and a single NGS analysis.
We use the FRELEX concept, an immobilized competitor antisense to determine the relative proportion of a target protein being bound by an individual Aptamarker. This is then directly quantified by qPCR analysis.
NeoVentures Biotechnology Europe provides partners with commercial access of Aptamarkers for their targets for diagnostic applications.
NeoVentures Biotechnology Europe is prepared to provide partners with commercial access of Aptamarkers for their targets for diagnostic applications.
