eagle-i The Ohio State UniversityThe Ohio State University

Quantitative Proteomics

eagle-i ID

http://eagle-i.rf.ohio-state.edu/i/00000176-2ea1-1432-ff38-acfe80000000

Resource Type

  1. Material analysis service

Properties

  1. Fee for service
    Yes
  2. Resource Description
    Quantitative Proteomics: The PSR offers both gel-based and non-gel-based methods to monitor protein differentiation expressions between samples. The PSR provides several approaches for the quantitative proteomics investigation. At least four biological replicates are required if statistical evaluation is needed. Label-Free Quantitation Using Spectral Counting: Spectral counting is a label-free quantitation technique, used in mass spectrometry, in which the number of spectra, identified for given peptides from the same protein in different biological samples, are counted and later integrated to determine the relative amount of the given protein. Quantitation also can be done by comparing peak areas for the protein from different biological conditions. TMT: TMT (tandem mass tag) is a non-gel-based labeling technique used to identify and quantify proteins/peptides from different sources in one single experiment, by using isotope-coded covalent tags that label the N-terminus and side chain amines of peptides from protein digestions. The ratios obtained by comparing the intensity of reported ions are used to calculate the ratios of a given peptide/protein. SILAC: SILAC (stable isotope labeling by/with amino acids in cell culture) is a mass spectrometric technique that detects differences in protein relative abundance among samples using stable isotopic labeling. Briefly, cells are differentially labeled by growing in light, medium or heavy media that substitutes certain amino acids with heavy isotope labeled ones (usually Arg, Lys and Leu). Metabolic incorporation of the amino acids into the proteins results in a mass shift for corresponding peptides. When the two samples are mixed, digested and analyzed by LC-MS/MS, the ratio of peak intensities in the mass spectrum for the doublets of unlabeled and labeled peptides reflects the relative protein abundance.
  3. Service Fee URL
    http://www.ccic.ohio-state.edu/MSP-Rates
  4. Contact
    Liwen Zhang
  5. Service Provided by
    The CCC Proteomics Shared Resource (PSR)
  6. Website(s)
    https://cancer.osu.edu/for-cancer-researchers/resources-for-cancer-researchers/shared-resources/proteomics
  7. Website(s)
    https://www.ccic.osu.edu/
  8. Part of Collection
    Campus Chemical Instrument Center
  9. Part of Collection
    The Ohio State University Comprehensive Cancer Center Collection
 
RDFRDF
 
Provenance Metadata About This Resource Record

    Copyright © 2016 by the President and Fellows of Harvard College
    The eagle-i Consortium is supported by NIH Grant #5U24RR029825-02 / Copyright 2016