Snapshot Proteomics™

Snapshot Proteomics™


Snapshot Proteomics™ uses microarrays that contain approximately 20,000 individual human proteins.  


Treating the array with a biological sample leads to changes at relevant protein targets.   Because the arrays and test samples are maintained in a near native state, enzymes and proteins maintain their activity allowing for signal amplification and greater sensitivity.  Similar to but distinct from a western blot, specific proteins are spatially separated into unique locations and the individual protein changes can be reported.


Inquire about Snapshot proteomics here:  Contact



Features of Snapshot Proteome Analysis 


The key to each Snapshot proteome analysis is an increase of both depth and breadth of coverage, and experimental reproducibility- allowing for innovative discovery within the proteome and specific pathways. Specifically monitored are:  

  •  post-translational modifications 
  •  protein-protein interactions 
  •  enzyme-substrate pairings 
  •  antibody specificity 
  •  small molecule-protein interaction 

These protein states are obtained by keeping the experiment in a pseudo-physiological context. By combining samples into treatment and control groups, contextual information relevant to the question is obtained allowing confirmation or discovery.   


Snapshot Proteomics


Services Offered


Rockland works closely with AVMBioMed to perform Snapshot Proteomics as a core technology that powers several services, each tailored to diverse scientific needs. Our services include far more than the raw data. You will also receive:  

  •  Bioinformatics analysis to reveal the underlying biology 
  •  A full report with detailed methods and explanation of results 
  •  Conference calls with our scientists who will personally present their findings, and unlimited technical support should additional questions arise 


Use Snapshot Proteomics to better inform your science, basic or applied. 

Questions of basic science

  • What proteins interact with my protein of interest (POI)? 
  • What are the substrates of my enzyme of interest? 
  • What are the enzymes that regulate my POI? 
  • How specific is my antibody? 
  • How does the proteome respond to overexpression/deletion/mutation of my POI? 



Click Here to Enlarge


Figure 1: Enzyme-substrate identification. Left image from array treated with cells knocked-out for a specific E3 ligase. Image on right from an identical array treated with control cells containing WT levels of that E3. Red box indicates a novel substrate of the ligase.


Questions of drug discovery

  • What proteins are hit by our compound (or therapeutic antibody)? 
  • How does the cellular proteome respond to the presence of our drug? 
  • What is the MOA of our drug, driving intended effect and side-effects? 



Click Here to Enlarge


Figure 2: Sorafenib-treated cells compared to DMSO-treated control cells. A) Phosphorylation of PDGFR and several MAPK members (red arrows) was decreased as expected: YAP1 and its effector kinases were increased in phosphorylation, consistent with being the driver of apoptosis as previously suggested. B) Changes to phosphorylation across the proteome in response to Sorafenib were examined for the presence of ontologies; those found were highly consistent with expectations for an anti-cancer drug operating through membrane receptors (note the presence of ubiquitin pathway, another PTM pathway known to drive cancer).


Biomarker Discovery


For drug development, truly useful biomarkers are specific to the compound, not the intended disease or molecular target.  Particularly in cases where traditional techniques (GWAS, NGS, MS/MS) have failed, Snapshot Proteomics (SP) can deliver novel and useful markers custom tailored to your project. 


In collaboration with a top-5 pharmaceutical company, SP was utilized to discover novel pharmacodynamic (PD) biomarkers in human sera, for an investigational analgesic known to inhibit prostaglandin synthesis.  The compound was in clinical trial, and previous attempts with alternative technologies were unsuccessful.



Click Here to Enlarge


Figure 3: SP used to identify PD biomarkers.
  Four different buffer conditions were evaluated, ranging from most natural (B1) to most chemically manipulated (B4).  Human sera were used to identify proteomic changes in ubiquitylation and phosphorylation in response to drug.  Three biomarkers were identified in common to all samples tested; all markers were consistent with the drug’s intended use and known MOA.  Markers identified were: phosphorylated UCN3, a protein known to bind G-protein receptors and linked to pain; phosphorylated GAGE1, a serum antigen involved in response to foreign agent and ubiquitylated SEPT6, a protein found in synaptic vesicles and the axon terminus.  FDR stands for false discovery rate. 



Related Products and Services:  


For all assay development services and information requests please inquire with one of our experts.


Contact Us