Discover What’s New in Proteomics at ABRF 2009

The 2009 ABRF Conference takes place February 7-10 in Memphis, Tennessee. Learn more about Thermo Scientific products and solutions for quantitative proteomics at Booths 401 and 403.

Don’t miss the Thermo Scientific technical workshop on Sunday evening. Topics will include quantification of phosphopeptides, and sample preparation strategies for detection of proteotypic peptides by electron transfer dissociation. Pick up a flyer at the booth for complete details. Register online, at the booth, or at the door; seating is limited.

Register for our ABRF workshop

Explore the Cutting Edge of Proteomics Research at US HUPO 2009

The 2009 conference of US HUPO takes place February 22-25 in San Diego, California. Thermo Scientific products and solutions for proteomics research will be on display in Booth 26. Our researchers will be presenting numerous posters in the poster sessions.

Be sure to join us for Thermo Scientific lunch and learn technical workshops on Monday and Tuesday. Register online, at the booth, or at the door; seating is limited.

Register for our US HUPO workshops

Recent Research

Unraveling molecular complexity of phosphorylated human cardiac troponin I by top down electron capture dissociation/electron transfer dissociation mass spectrometry

Cardiac troponin I (cTnI) is widely used as a serum biomarker of cardiac injury. In vivo function of cTnI is influenced by phosphorylation and proteolysis. However, cTnI contains twelve serine, eight threonine, and three tyrosine residues, presenting a challenge for unequivocal identification of phosphorylation sites and quantification of positional isomers. This study employed top-down electron capture dissociation (ECD) and electron transfer dissociation (ETD) on a high-resolution Fourier transfer mass spectrometry (FTMS) to unravel the molecular complexity of cTnI and facilitate the understanding of cardiac regulatory mechanisms.

View the article in Molecular and Cellular Proteomics online

Application Note 445 – Quantitative Profiling of DNA Damage Response Proteins Using iTRAQ Labeling and the LTQ Orbitrap XL

Proteins often undergo changes in concentration or composition in response to DNA damage or cellular stress. This application note illustrates a methodology for qualitative and quantitative assessment of such changes, using phosphoprotein enrichment and mass spectrometric analysis. More than 500 proteins from A549 cell lysates were identified in this study. Separate analysis of enriched phosphoproteins increased the overall number of proteins identified by 145.

Read application note 445 (.pdf 748 KB)

Application Note 444 – A Robust and Sensitive Workflow for Label-Free, Quantitative Identification of Differentially Expressed, Endogenous Peptides in Human Serum

This application note describes the development of a workflow specifically geared toward the efficient recovery, quantitation, and identification of endogenous peptides from blood. The workflow employs a combination of up-front batch sample preparation and on-line liquid chromatography coupled with high-resolution tandem MS using HCD and CID fragmentation in an Thermo Scientific LTQ Orbitrap XL. Quantitative differential analysis of the endogenous peptides was carried out using label-free analysis and Thermo Scientific SIEVE software. The workflow was used to investigate the quantitative differences in endogenous peptides recovered from maternal serum in normal and Trisomy 21 (Down’s Syndrome) pregnancies.

Read application note 444 (.pdf 1.1 MB)

Application Note 443 – Quantitative Proteomic Workflow for Discovery of Early Rejection Kidney Transplant Peptide Biomarkers

This note describes a two-stage approach for the identification peptides that might serve as early markers of rejection of kidney transplants. High-resolution, accurate-mass MS/MS was used to identify differentially expressed endogenous peptides in urine. The resulting data was used to increase the efficiency and accuracy of quantitative SRM assays on a triple quadrupole mass spectrometer. The result was identification of a specific endogenous peptide in early and full rejection conditions that was not present in the stable patient samples.

Read application note 443 (.pdf 703 KB)

New LSMS Abstracts Database Rev 1.9

The latest revision of the Thermo Scientific Life Science MS Abstracts Database CD now includes:

• Over 3900 mass spec abstracts
• 1950 proteomics application abstracts
• 140 PTM analysis abstracts
• 240 biomarker discovery abstracts
• 260 MALDI application abstracts
• Top-down, bottom-up, and high-throughput protein ID

This release of the abstracts CD includes advanced search features.  Request your copy today.

Important Proteomics Events

Be sure to mark your calendars to attend the following proteomics events:

ABRF – February 7-10, Memphis, Tennessee, USA
US HUPO – February 22-25, San Diego, California, USA
Berlin Proteomics Forum – March 29-April 2, Berlin, Germany
ASBMB – April 18-22, New Orleans, Louisiana, USA
ETP – May 14, Vancouver, Canada
ASMS – May 31-June 4, Philadelphia, Pennsylvania, USA
EuPA – June 14-17, Stockholm, Sweden
MediLS Summer School – June 27-July 2, Split, Croatia

Give us your feedback!

The goal of this newsletter is to provide you timely, relevant information about new tools and workflows in proteomics research. For this reason, we actively solicit contributions from our readers and other investigators describing new developments in proteomics theory and practice. Proteome Digest will also feature upcoming proteomics seminars, workshops and symposia.

We invite you to give us your feedback; comments and contributions are always welcome!