Fluorosequencing moves beyond genomics as the world's first single- molecule protein sequencer.
Fluorosequencing goes where existing technologies cannot, empowering scientists to ask key questions that will help overcome difficult-to-treat diseases.
Fluorosequencing brings all the advantages of next- generation DNA sequencing to proteins, combining leading-edge digital quantification with high sensitivity and throughput. It is ideal for quantifying vast numbers of peptides in ultra-low sample concentrations, such as those found in tumor biopsies, or in extremely rare samples.
1. Liu, Y., Beyer, A. & Aebersold, R.Cell165, 535–550(2016).
Fluorosequencing is 1 million times more sensitive than mass spectrometry. Assuming a factor of at least 1000, this translates into extremely low sample amounts: the difference between needing 1/4th of a pancreas or sampling with a needle for biopsy material.
Our technology achieves a scalable throughput that was previously unattainable, empowering researchers and clinicians to identify hundreds of millions or even billions of peptide molecules on a single glass slide.
Fluorosequencing enables researchers to compare proteins in the same sample – and across experiments – without need for external calibrants. Unlike other technologies, fluorosequencing quantifies peptides and proteins by counting molecular observations.
Our technology can discriminate peptides and proteins across a large range of heterogeneity and abundances (up to 10^6 range). Identify peptides existing in extremely diverse backgrounds, such as antigens on tumor surfaces or a low abundant phosphorylation event on a protein.
With help from a reference database, only a few amino acids are needed to uniquely identify a protein in a proteome.
EXAMPLE: CATALOGING ALL THE PROTEINS OF A SINGLE CELL
The protein sample is digested, creating hundreds of millions or billions of peptides.
Select amino acids are Fluorescently labeled.
The peptides are immobilized.
Image capture establishes baseline fluorescence.
The sequence is determined by the intensity of the fluorescence.
Subsequent cycles of imaging and Edman chemistry are conducted, usually 15-20 cycles. Fluorescence is analyzed and amino acids are identified to create a fluorosequence.
The fluorosequence is matched in a database to identify which protein the peptide came from.
Highly Parallel Single-Molecule Identification of Proteins in Zeptomole-Scale Mixtures
“Fluorosequencing: Concept, Features and Benefits”
“Mapping the Residue Positions of a Protein’s Post- Translational Modification”