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MALDI mass spectrometry

eagle-i ID


Resource Type

  1. Material analysis service


  1. Fee for service
  2. Resource Description
    "Purpose: Determine masses of purified peptides or proteins in solution. MALDI mass analysis is feasible over a wide mass range and can help identify the extent of post-translational modifications such as oxidation, glycosylation, and phosphorylation. It is the method of choice to check integrity of synthetic peptides, peptides from fractions of HPLC separations, and integrity of recombinant proteins. While some salts and buffers are tolerated, it may be necessary to 'clean up' the sample prior to analysis if buffer components suppress the mass signal. Requirements: Purified peptides for routine analysis should be between 0.5-5 pmoles/µl in 0.1% TFA (sample also may contain up to 50% acetonitrile). Proteins should be 10 pmoles/µl, preferably in 20 mM NH4HCO3. It is especially important to avoid the following: Phosphate buffer >20 mM, most detergents >0.1% or SDS >0.01%, alkali metal salts >1M, glycerol >1%, Tris buffer >10 mM, guanidine or urea >1 M, or sodium azide >1 mM. Results: Printouts of the masses found and a printout of the standard used for the calibration of the instrument in PDF file format."
  3. Service Fee URL
  4. Related Resource
    Applied Biosystems Voyager-DE® PRO MALDI TOF Mass Spectrometer
  5. Service Provided by
    Proteomics and Metabolomics Facility (Wistar)
  6. Website(s)
  7. Related Technique
    Post translational modification identification by mass spectrometry
  8. Related Technique
    Matrix-assisted laser desorption ionization time-of-flight mass spectrometry
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