Adelaide Proteomics Centre


The Adelaide Proteomics Centre offers researchers in South Australia a state-of-the-art proteomics facility. Its combination of internationally recognised expertise, advanced equipment and customer service focus is unique. It offers the latest proteomics technology to researchers from all fields of biological science.

The centre is a joint venture of the University of Adelaide and SA Pathology, established with support from the Australian Cancer Research Foundation. It has been awarded $900,000 in Commonwealth funding to further build capacity in MALDI Tissue Imaging Mass Spectrometry and establish a national Tissue Imaging Mass Spectrometry node for Bioplatforms Australia.


Products and services

Mass Spectrometry     Gel Electrophoresis

The Adelaide Proteomics Centre has the latest mass spectrometry technology to identify proteins and characterize their post-translational modifications, such as glycosylation and phosphorylation. The centre is also equipped to detect and quantify the expression profiles of proteins in complex mixtures using techniques such as label and label free quantification mass spectrometry and gel electrophoresis techniques such as DIGE and native 2D.


Type Manufacturer Model
Imaging and Mass Spectrometry
nanoLC-ESI-QTOF-MS Bruker Daltonics Impact II™ QTOF
nanoLC-ESI-Oribitrap-MS Thermo Scientific LTQ Orbitrap XL
nanoLC-ESI-IonTrap-MS Bruker Daltonics Amazon 3D Ion Trap
ESI-IonTrap-MS Bruker Daltonics HCT Ultra Ion Trap
MALDI UltrafleXtreme Bruker Daltonics UltrafleXtreme
MALDI Ultraflex III Bruker Daltonics Ultraflex III TOF/TOF
LC-MALDI Spotter Bruker Daltonics Proteineer FC
Chemical Inkjet Printer Shimadzu Biotech Chip-1000
Spot Picking Robot Amersham Biosciences Ettan Spot Picker
ImagePrep Bruker Daltonics ImagePrep
Protein separation
Free Flow Electrophoresis FFE Weber Pro-Met-HEUS
Off-gel IEF (dPC Fractionator) Protein Forrest SB-106
HPE Tower Electrophoresis Gel Company PPT-001-TI
IPGphor Pharmacia IPGphor
Quantitative 2D Electrophoresis
DIGE Imager GE Healthcare Ettan DIGE Imager
Capillary Electrophoresis Beckman Coulter P/ACE MDQ
Name Description
Protein Indentification by mass spectrometry

Protein samples are digested with trypsin and the resulting peptides analysed by mass spectrometry with high accuracy.

Selected peptides are fragmented inside the mass spectrometer (tandem MS) to produce fragment ions which give information about the peptide’s sequence.

The combined data are matched against protein sequence databases to determine the protein’s identity.

Label and label free quantification of complex protein mixtures

In recent time’s technical advances in mass spectrometry been significant. The Increased scan rate and resolution of instruments has allowed for great improvements in the sensitivity and depth of coverage of complex proteomes, coupled with improvements in processing algorithms and quantification analysis programs.

These factors combined have allowed for the identification and quantification of thousands of proteins per sample using nano-flow liquid chromatography mass spectrometry.

Samples can be labelled and analysed, utilizing mass tags for the quantification of multiple samples within a single mass spectrometry run, or analysed label free over multiple runs.

Adelaide Proteomics Centre can offer both data dependent and data independent mass spectrometry.

Targeted quantification of peptides/ proteins

Quantification isotopically labelled (absolute quantification) or un-labelled (relative quantification) peptides/ proteins can be achieved using the mass spectrometry technique of parallel reaction monitoring (PRM). PRM is a highly sensitive form of targeted mass spectrometry that allows the relative quantification peptides.

During a PRM run peptides are targeted for fragmentation and detection using their observed precursor ion mass within a QTOF mass spectrometer, taking into account the mass and charge of the peptides (known as m/z).

During PRM analysis data is matched back to a spectral library containing previously acquired fragmentation spectra of the peptides of interest ensuring specificity, and area under the curve measurements are calculated for the detected fragment ions.

Sensitivity is achieved in the technique by targeting and fragmenting only specific masses of interest.

Two-Dimensional Electrophoresis

Two-dimensional electrophoresis (2-DE) provides a method for separating complex protein mixtures based on two intrinsic properties of proteins: their isoelectric points and molecular weights.

In the first dimension, termed isoelectric focusing (IEF), the proteins are separated out on a specified pH gradient. In the second dimension the proteins are separated according to their molecular weight by SDS-PAGE.

The resulting 2-DE can be stained or transferred for blotting applications. Labelling of samples with fluorescent dyes can be used to detect changes in protein expression between two samples, referred to as Difference In-Gel Electrophoresis (DIGE).


Dr Peter Hoffmann



The University of Adelaide
North Terrace Campus
Level 1, Molecular Life Sciences
Frome Rd
Adelaide SA 5000