From a pinhole to a panorama

Our approach starts with proprietary engineered nanoparticles developed to maximize proteomic insights – simply and robustly

Proteins are functional drivers of biology and thus key indicators of status in any living organism. To truly understand biology, we must empower researchers with the tools necessary to discover, annotate, and understand the rich universe of the proteome.

For decades, a critical limiting factor has been the inability to access the proteome in an unbiased, deep manner rapidly and at the scale necessary to survey and understand its diversity.

To build a more transformative view of the proteome, we had to create a new technology. One that provides a new lens on the proteome, enabling researchers to see the breadth, depth and dynamic nature of protein diversity across populations and time. Seer developed a proprietary approach by engineering nanoparticles with unique physicochemical properties that enable deep and unbiased interrogation of the proteome in complex samples such as plasma, in a rapid and scalable workflow.

We aim to empower researchers to see more of the proteome and understand more of its diversity

Population Scale

The unique properties of Seer’s engineered nanoparticles enable you to explore the proteome in new ways

Broad affinity range

Broad affinity range

Reproducible and selective binding without prior knowledge, using engineered nanoparticles that allow unbiased interrogation of proteoforms

Quantitative compression of the dynamic range renders low abundant proteins visible to detectors

Tunable physiochemical properties

Tunable physiochemical properties

Nearly infinite combination of distinct nanoparticle designs to survey the full richness of proteoform diversity

Removes complexity of experiments

Robust, simple, and scalable

Robust, simple, and scalable

Reproducible performance across samples, labs, and experiments

Automated, easy to use, and scalable workflow eliminates the need for lengthy and costly depletion and fractionation required with existing processes, making it simple to see the proteome complexity