The Proteomics services are closing operations. Effective
immediately, October 27, 2008, the Proteomics Facility is no longer accepting
new samples or beginning new projects. We regret that this action is necessary
and want to express our appreciation for the contributions of all those
individuals and organizations that supported us in the past. If you have
questions, please contact
Vance Morgan, Ph.D, at tvmorgan@partners.org.
The Proteomics Facility
employs high throughput parallel processing of samples and state
of the art liquid chromatography - electrospray mass spectrometry
to elucidate the protein composition of source materials ranging
in complexity from gel spots to whole cell lysates.
The Proteomics center
at HPCGG provides researchers with protein biochemistry
and mass spectrometry resources in support of research
projects. The goal of the Proteomics Group at HPCGG
is to provide information on both the qualitative and
semi-quantitative protein content and protein modifications
using the latest technology available.
The mass spectrometers at our facility include
a ThermoFisher LTQ-XL (linear ion trap) and a ThermoFisher LTQ-FT (hybrid
high resolution ion trap-FT-MS system). Both are equipped with Famos
low volume autosamplers, microspray sources and nanospray sources. The facility also has state of the art nanospray and microspray HPLC column and spray tip manufacturing
facilities with which to generate, on demand, in any custom configuration,
LC-MS columns. Also available is an AKTA Explorer Bio-HPLC
workstation, and gel electrophoresis equipment for protein and peptide
separation.
We offer a wide range of services to our clients ranging from advanced preparative HPLC and processing
of complex protein mixtures to single gel spot digest
analysis. Mass spectrometry analysis is by 1D and / or 2D LC-MS/MS.
Analysis of data for post-translational modifications,
protein profiling, and protein ID are available.
The cost for a standard analysis includes in-gel or in-solution digestion using trypsin. Peptides are analyzed by LC/MS/MS. Proteins are identified by comparison of the tandem MS/MS of experimentally found peptides with predicted MS/MS spectra in the appropriate sequence database using the SEQUEST algorithm. In special cases we can identify experimental peptides that do not appear in protein sequence databases.
We can also identify modified proteins.
In general, if a protein band or spot is visible by Coomassie or Sypro Ruby staining, it should be able to be identified. Duplicate gel bands may be combined.
If you must use silver stain, the Silverquest stain from Invitrogen is Mass Spec friendly.
Call to discuss your project before sending samples.
Keratin is unavoidable, but the less the better
Wear gloves during sample preparation
Wash everything that will come in contact with your sample
Avoid using molecular weight cut-off filters. If you must, wash them thoroughly. They are often a source of synthetic polymer contamination.
Avoid using detergents such as Triton-X and CHAPS.
Minimize salt and buffer concentration in the sample. We can suggest suitable alternatives.
We welcome large scale programs
and would be happy to discuss how our core could
offer support by means of letters of support for grant applications.
Contact Information:
Soumya Vemuri
Research Assistant
(617) 768-8485
Email: svemuri@partners.org
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