Services and Rates

Services

A highly purified protein, submitted either in-gel or in-solution, is digested with trypsin then analyzed by MALDI-TOF/TOF or LC-MS/MS, depending on protein purity and amount. Data is searched against a publicly available protein database using either Mascot or Sequest search engines. Data is processed in Protein Pilot or Proteome Discoverer.
Identification/localization of modifications on highly purified proteins, which can be submitted either in-gel or in-solution. Modifications may include:
  1. Post-translational modifications (PTMs) such as phosphorylation, ubiquitination, acetylation, and glycosylation. If you're interested in a specific modification, please contact us so that we may direct you to sample preparation protocols that could be used to optimize its detection.
  2. Covalent modifications such as drugs or other compounds. The customer must provide us with the compound formula of these modifications.
Proteins are typically digested with trypsin then analyzed by LC-MS/MS. Data is searched against a publicly available or user provided protein database using either Mascot or Sequest search engines. Data is processed in Protein Pilot or Proteome Discoverer.
Identification/localization of phosphorylation sites. Several methods have been optimized to specifically enrich for phosphopeptides after proteolytic digestion. Two are employed at the UNC Proteomics Facility: IMAC and TiO2 enrichment. There are two phosphoproteomic workflows:
  1. Phosphorylation site mapping of a highly purified protein.
  2. Large-scale phosphoproteomic analysis.
After trypsin digestion, phosphopeptides are enriched and the enriched sample is analyzed by LC-MS/MS. The gradient length may be extended depending on sample complexity. Afterward, data is searched against a publicly available protein database using either Mascot or Sequest search engines. Data is processed in Proteome Discoverer or MaxQuant.
Identification of binding partners of a specific, immunoprecipitated protein. There are critical sample preparation steps that must be considered before submitting these types of samples, so please contact the staff to discuss the project prior to sample preparation. Each sample MUST be submitted with a proper control.

Depending on the IP protocol, immunoprecipitated proteins are digested using an in-gel or on-beads digestion protocol, then analyzed by LC-MS/MS. The gradient length may be extended depending on sample complexity. Afterward, data is searched against a publicly available protein database using either Mascot or Sequest search engines. Data is processed in Proteome Discoverer or MaxQuant. Proteins identified in the control are compared to proteins identified in the sample.
Identification of proteins in a complex mixture, which can be submitted either in-gel or in-solution. Most of the time, this service is coupled with some type of quantitation to compare the proteome of a sample to a control. Proteins are digested with typsin (in-gel or in-solution), then analyzed by LC-MS/MS using the QExactive HF. Typically, a longer gradient is used to identify as many proteins as possible. Afterward, data is searched against a publicly available protein database using either Mascot or Sequest search engines. Data is processed in Proteome Discoverer or MaxQuant.

This service can be coupled with offline fractionation to further maximize the number of protein identifications. Please contact the staff for details.
Several of our services can be performed quantitatively to determine differential changes of proteins or PTMs between multiple samples. Quantitiative methods include:

  1. Stable Isotopic Labeling by Amino Acids in Cell Culture (SILAC). Customers are required to purchase SILAC reagents and perform the SILAC incorporation themselves. Prior to large-scale experiments, incorporation testing by LC/MS/MS analysis must be performed to determine the incorporation efficiency.
  2. Isobaric tagging (iTRAQ or TMT). The facility provides the labels and will perform the labeling step for the customer.
  3. Label-free using area under the curve or spectral counting. No additional sample preparation required.
  4. AQUA peptides for targeted quantitation. Customers are responsible for purchasing the peptides.
Quantitative data is generated using Proteome Discoverer or MaxQuant.
Protein or peptides are submitted in-solution, please contact us for buffer and concentration requirements. Intact molecular weight can be determined by either using the MALDI-TOF/TOF (low resolution) or Orbitrap (high resolution) instruments, depending on the molecular weight. Other molecules such as polymers, oligonucleotides and synthetic proteins/peptides may be submitted.

Rates

Rates effective as of 2/1/2016

Please note that most projects are a combination of these services. Estimations of our most common services are also listed.

To request a quote, please contact Associate Director,.

UNC 
System
External
Academic
External
For-Profit
Trypsin digestion $40 $60 $80
Sample clean-up (C18 spin column, zip tip, etc) $30 $45 $60
Phosphopeptide enrichment $100 $150 $200
Isobaric tag (TMT or iTRAQ), per sample $150 $225 $300
Additional sample prep procedures, hourly $50 $75 $100
UNC 
System
External
Academic
External
For-Profit
5800 MALDI-TOF/TOF, protein digest, per sample $50 $75 $100
5800 MALDI-TOF/TOF, intact mass (1-3 samples), each $40 $60 $80
5800 MALDI-TOF/TOF, intact mass (add'l samples, >3), each $20 $30 $40
LTQ-Orbitrap Velos, per hour $100 $150 $200
QExactive HF, per hour $150 $225 $300
LC-MALDI-TOF/TOF contact
UNC 
System
External
Academic
External
For-Profit
Data analysis, per hour $50 $75 $100
UNC 
System
External
Academic
External
For-Profit
5800 MALDI-TOF/TOF training $200 $300 -
5800 MALDI-TOF/TOF usage, per hour $80 $120 -
Additional training, per hour $50 $75 $100
UNC 
System
External
Academic
External
For-Profit
Protein ID from gel, MALDI-TOF/TOF $140 $210 $280
Protein ID from gel, LTQ-Orbitrap Velos $190 $285 $380
Phosphorylation site mapping of single protein from gel $340 $510 $680
Protein characterization from gel (e.g., detection of a modification) $290 $435 $580
Identification of binding partners from gel, 2 (control + sample) $760 $1140 $1520
Global quantitative analysis, 4 samples (in-solution digest, sample clean-up, iTRAQ labeling, LC-MS/MS, quantitative data analysis) $1730 $2595 $3460
  1. Appalachian State University
  2. East Carolina University
  3. Elizabeth City State University
  4. Fayetteville State University
  5. North Carolina A&T State University
  6. North Carolina Central University
  7. North Carolina State University
  8. UNC Asheville
  9. UNC-Chapel Hill
  10. UNC Charlotte
  11. UNC Greensboro
  12. UNC Pembroke
  13. UNC Wilmington
  14. Western Carolina University
  15. Winston-Salem State University