Monash Proteomics & Metabolomics Facility

Provides detailed information of any PTM of interest on a single or global protein level!

The vast majority of proteins are post-translationally modified (e.g. phosphorylation or glycosylation). Mass spectrometry is one of the few techniques that allow the precise identification and quantification of virtually every PTM on a global proteomics scale.

Quantifies as many lipids as possible between samples!

We provide untargeted, quantitative analysis of all hydrophobic metabolites (lipids) and identify significant molecular features.

These analyses are suited for investigation of lipid biochemistry in cell or animal models, and for biomarker discovery in clinical samples.

Quantifies as many metabolites as possible between samples!

We provide comparative measurements of metabolites involved in central metabolic pathways (such as amino acid, carbohydrate, lipid, nucleotide and cofactor metabolism) as well as untargeted detection and identification of significant molecular features that may represent novel biomarkers or biochemical phenotypes in cell cultures, tissues, biofluids or other sample types.

This technique can also be used to identify protein-bound ligands!

Identifies interacting domains within proteins and protein complexes!

Chemical cross-linker reagents can be used to covalently link adjacent domains within proteins and protein complexes. Identifying the cross-linked domains/peptides by high-resolution mass spectrometry provides a powerful tool to reveal interacting regions of protein complexes. CX-MS can also be used to analyze naturally occurring crosslinks such as disulphide bridges.

Deciphers the complete amino acid sequence of antibodies and proteins!

Using a combination of bottom-up proteomics with intact mass analysis and N-terminal sequencing, we can determine the full amino acid sequence of proteins and antibodies (including their variable regions).

Determines the exact mass of any molecule of interest!

The determination of intact protein masses and their top-down fragments enables us to (i) analyze the exact size of proteins, (ii) confirm the presence of polymorphisms, PTMs, truncations or other mutations, and (iii) distinguish between protein isoforms and splice forms.

Identifies the exact N-terminal amino acid sequence of any protein!

N-terminal sequencing is an unequivocal sequencing method based on the Edman degradation chemistry which will confirm the identity of a protein, the exact N-terminus of a protein and can also be used to determine the purity of proteins.

N-Terminal Sequencing can have up to 4 steps

Step 1: Cysteine Detection (Optional, per sample, determined by customer)

Step 2: Sample Clean-up (Optional, per sample, determined by staff)

Step 3: Start-up (Fixed amount charged per sample) (Includes Standard and System set up)

Step 4: Cycles (Number of residues to sequence) (variable per sample, determined by customer)

If a protein sample contains more than one protein, the analysis will show a mixture of amino acids in each cycle.

No sequence will be detected if the protein is N-terminally blocked. More than 50% of all eukaryote proteins are blocked. Common N-terminal blocking groups include pyroglutamate, N-acetyl groups such as acetyl¬serine or acetyl-threonine and N-formylated amino acids. 

How to get access?:

Please register an account with iLab and log in to https://monash.ilab.agilent.com/

Proteomics services can be requested via the request form

https://monash.ilab.agilent.com/service_item/new/4448?spt_id=11826

Identifies and quantifies as many phosphorylated peptides as possible! An indispensable tool for analyzing kinases and signal transduction networks

After enriching phosphorylated peptides with titanium oxide beads, we are using data-dependent or data-independent acquisition mass spectrometry to globally determine changes in the phosphoproteome.

Identifies as many proteins in a sample as possible!

Isolated proteins or even entire proteomes are analyzed by LC-MS/MS. This methodology can be used to (i) identify interaction partners, (ii) verify polymorphisms and other mutations, (iii) analyze secreted proteins, (iv) reveal novel proteomes and (v) confirm the identity of purified proteins, synthesized peptides or gel bands.

We are using Label-Free Quantification (LFQ) as well as Data-Independent Acquisition Mass Spectrometry (DIA-MS, often referred as SWATH-MS) in addition to several label-based workflows to analyze global proteomic changes between any number of biological samples. More targeted methods such as Multiple Reaction Monitoring (MRM) or Parallel Reaction Monitoring (PRM) are also in place to quantify selected proteins with unprecedented sensitivity and accuracy.

Provides absolute quantitative measurements of lipids of interest!

We measure hydrophobic metabolites (lipids) of interest in any number of samples using TripleQuadrupole mass spectrometers. Absolute quantitative measurements can be achieved by adding isotopically labelled compounds to the samples.

Enables functional studies of metabolic pathways!

Take your metabolism studies to the next level by including stable isotope labelled tracers to measure flux through metabolic pathways. These tracer-based approaches can be combined with our metabolomics workflows to get an accurate measurement of flux through a pathway of interest, or to more broadly map the active metabolic network of a cellular system.

Provides absolute quantitative measurements of metabolites of interest!

We measure metabolites of interest in any number of samples using TripleQuadrupole mass spectrometers. Absolute quantitative measurements can be achieved by adding isotopically labelled compounds to the samples.

Only interested in a few specific metabolites and lipids? No worries. We have targeted methods for the following pathways and classes:

Central carbon metabolism (Glycolysis, PPP and TCA cycle)

Amino Acids

Bile acids

Thiol metabolites (glutathione)

Ceramides

Short-chain fatty acids

Lipid mediators

Methylated nucleotides

Identifies as many proteins in a sample as possible!

Isolated proteins or even entire proteomes are analyzed by LC-MS/MS. This methodology can be used to (i) identify interaction partners, (ii) verify polymorphisms and other mutations, (iii) analyze secreted proteins, (iv) reveal novel proteomes and (v) confirm the identity of purified proteins, synthesized peptides or gel bands.

We are using Label-Free Quantification (LFQ) as well as Data-Independent Acquisition Mass Spectrometry (DIA-MS, often referred as SWATH-MS) in addition to several label-based workflows to analyze global proteomic changes between any number of biological samples. More targeted methods such as Multiple Reaction Monitoring (MRM) or Parallel Reaction Monitoring (PRM) are also in place to quantify selected proteins with unprecedented sensitivity and accuracy.

Provides detailed information of any PTM of interest on a single or global protein level!

The vast majority of proteins are post-translationally modified (e.g. phosphorylation or glycosylation). Mass spectrometry is one of the few techniques that allow the precise identification and quantification of virtually every PTM on a global proteomics scale.

Identifies interacting domains within proteins and protein complexes!

Chemical cross-linker reagents can be used to covalently link adjacent domains within proteins and protein complexes. Identifying the cross-linked domains/peptides by high-resolution mass spectrometry provides a powerful tool to reveal interacting regions of protein complexes. CX-MS can also be used to analyze naturally occurring crosslinks such as disulphide bridges.

Identifies and quantifies as many phosphorylated peptides as possible! An indispensable tool for analyzing kinases and signal transduction networks

After enriching phosphorylated peptides with titanium oxide beads, we are using data-dependent or data-independent acquisition mass spectrometry to globally determine changes in the phosphoproteome.

Deciphers the complete amino acid sequence of antibodies and proteins!

Using a combination of bottom-up proteomics with intact mass analysis and N-terminal sequencing, we can determine the full amino acid sequence of proteins and antibodies (including their variable regions).

Determines the exact mass of any molecule of interest!

The determination of intact protein masses and their top-down fragments enables us to (i) analyze the exact size of proteins, (ii) confirm the presence of polymorphisms, PTMs, truncations or other mutations, and (iii) distinguish between protein isoforms and splice forms.

Identifies the exact N-terminal amino acid sequence of any protein!

N-terminal sequencing is an unequivocal sequencing method based on the Edman degradation chemistry which will confirm the identity of a protein, the exact N-terminus of a protein and can also be used to determine the purity of proteins.

N-Terminal Sequencing can have up to 4 steps

Step 1: Cysteine Detection (Optional, per sample, determined by customer)

Step 2: Sample Clean-up (Optional, per sample, determined by staff)

Step 3: Start-up (Fixed amount charged per sample) (Includes Standard and System set up)

Step 4: Cycles (Number of residues to sequence) (variable per sample, determined by customer)

If a protein sample contains more than one protein, the analysis will show a mixture of amino acids in each cycle.

No sequence will be detected if the protein is N-terminally blocked. More than 50% of all eukaryote proteins are blocked. Common N-terminal blocking groups include pyroglutamate, N-acetyl groups such as acetyl¬serine or acetyl-threonine and N-formylated amino acids. 

How to get access?:

Please register an account with iLab and log in to https://monash.ilab.agilent.com/

Proteomics services can be requested via the request form

https://monash.ilab.agilent.com/service_item/new/4448?spt_id=11826

Quantifies as many metabolites as possible between samples!

We provide comparative measurements of metabolites involved in central metabolic pathways (such as amino acid, carbohydrate, lipid, nucleotide and cofactor metabolism) as well as untargeted detection and identification of significant molecular features that may represent novel biomarkers or biochemical phenotypes in cell cultures, tissues, biofluids or other sample types.

This technique can also be used to identify protein-bound ligands!

Provides absolute quantitative measurements of metabolites of interest!

We measure metabolites of interest in any number of samples using TripleQuadrupole mass spectrometers. Absolute quantitative measurements can be achieved by adding isotopically labelled compounds to the samples.

Only interested in a few specific metabolites and lipids? No worries. We have targeted methods for the following pathways and classes:

Central carbon metabolism (Glycolysis, PPP and TCA cycle)

Amino Acids

Bile acids

Thiol metabolites (glutathione)

Ceramides

Short-chain fatty acids

Lipid mediators

Methylated nucleotides

Enables functional studies of metabolic pathways!

Take your metabolism studies to the next level by including stable isotope labelled tracers to measure flux through metabolic pathways. These tracer-based approaches can be combined with our metabolomics workflows to get an accurate measurement of flux through a pathway of interest, or to more broadly map the active metabolic network of a cellular system.

Quantifies as many lipids as possible between samples!

We provide untargeted, quantitative analysis of all hydrophobic metabolites (lipids) and identify significant molecular features.

These analyses are suited for investigation of lipid biochemistry in cell or animal models, and for biomarker discovery in clinical samples.

Provides absolute quantitative measurements of lipids of interest!

We measure hydrophobic metabolites (lipids) of interest in any number of samples using TripleQuadrupole mass spectrometers. Absolute quantitative measurements can be achieved by adding isotopically labelled compounds to the samples.