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Related Experiment Video

Updated: Dec 15, 2025

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

Simple Method to Quantify Protein Abundances from 1000 Cells.

Burcu Vitrinel^1,2, Dylan E Iannitelli², Esteban O Mazzoni^2,3

¹Center for Genomics and Systems Biology, Department of Biology, New York University, New York, New York 10003, United States.

|July 9, 2020

Summary

This summary is machine-generated.

Researchers developed a new proteomics workflow to quantify over 2500 proteins from just 1000 mammalian stem cells. This method offers high reproducibility and accuracy for minimal sample input, advancing single-cell proteomics.

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Published on: November 15, 2017

Related Experiment Videos

Last Updated: Dec 15, 2025

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

Counting Proteins in Single Cells with Addressable Droplet Microarrays

Counting Proteins in Single Cells with Addressable Droplet Microarrays

Published on: July 6, 2018

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Area of Science:

Proteomics
Molecular Biology
Stem Cell Research

Background:

Single-cell transcriptomics has advanced rapidly.
A parallel need exists for protein quantification from minimal cell numbers.
Existing proteomics methods often require large cell inputs.

Purpose of the Study:

To establish a robust proteomics workflow for minimal cell samples.
To enable protein quantification from as few as 1000 mammalian stem cells.
To provide a reproducible and accurate method for low-input proteomics.

Main Methods:

Integrated and optimized recent chemical peptide labeling techniques.
Developed a workflow requiring only standard cell lysis equipment.
Quantified protein expression levels from minimal cell inputs.

Main Results:

Successfully quantified >2500 proteins from 1000 mammalian stem cells with high reproducibility.
Identified differentially expressed proteins with small fold changes.
Demonstrated comparable dynamic range and accuracy to standard proteomics methods.
Validated the protocol on mouse embryonic stem cells, motor neurons, and FACS-purified Ciona cells.

Conclusions:

The developed proteomics workflow is straightforward and accurate for minimal input samples.
This method addresses the need for single-cell level protein quantification.
The protocol is versatile and applicable to various biological systems.