Characteristics of ITRAQ, TMT, and SILAC

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LABEL-BASED PROTEIN QUANTFICATION iTRAQ, TMT, SILAC introduction of itraq, tmt and silac iTRAQ Isobaric Tags for Rela�ve and Absolute Quan�ta�on (iTRAQ) technology u�lizes isobaric reagents to label the primary amines of pep�des and proteins. The iTRAQ reagents usually consist of an N-methyl piperazine reporter group, a balance group, and an N-hydroxy succinimide ester group that is reac�ve with the primary amines of pep�des. The balance groups present in each of the iTRAQ reagents func�on to make the labeled pep�des from each sample isobaric and the quan�fica�on is facilitated through analysis of reporter groups that are generated upon fragmenta�on in the mass spectrometer.

Amine specific pep�de reac�ve group(NHS)

Report Ion

Balancer Group

There are currently two mainly used reagents: 4-plex and 8-plex, which can be used to label all pep�des from different samples/treatments.

TMT Mass Reporter

Protein Reac�ve Group

Tandem Mass Tags (TMT) can be used to iden�fy and quan�fy proteins in different kinds of samples. Each TMT tagging reagent is composed of an amine-reac�ve NHS-ester group, a spacer arm and an MS/MS reporter. And the isobaric tagging reagent within a set has the same nominal parent (precursor) mass.

Mass Normalizer

Eleven tags are available in TMT to label almost any pep�de or protein samples. Using TMT, mul�plex analysis, �me efficiency, and control over technical varia�ons can all be achieved.

SILAC Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) technique performs protein labeling by adding light, medium, or heavy stable isotope-labeled essen�al amino acids (lysine and arginine) to cell culture media. Through the normal metabolism of the cell, a�er 5-6 mul�plica�on cycles, the stable isotope-labeled amino acids are completely incorporated into the newly synthesized proteins of the cell, so that the newly synthesized proteins are labeled with stable isotopes. In this way, the area size of isotope peak type in mass spectrogram was compared for rela�ve quan�fica�on, and the sequence of pep�de was determined by secondary harmonic diagram for protein iden�fica�on.

workflow of itraq, tmt and silac iTRAQ Pep�des

iTRAQ Labelling 114

191

PRG

115

190

PRG

116

189

PRG

117

188

PRG

Proteins

SILAC

Pep�des

iTRAQ Labelling Grow Cells in Medium with Light Isotopes

TMT10-126

TMT10-127N

TMT10-128C

Lysate Cells to Extract Proteins

TMT10-129N

Labeled Pep�de Mixture

TMT10-129C

TMT10-130N

Combine Lysates 1:1 Frac�onate

HPLC Separa�on of Pep�de Mixture TMT -130C 10

TMT10-131

MALDI MS/MS Analysis

Trypsin Diges�on

Intensity

HPLC Separa�on of Pep�de Mixture

Intensity

116 115

LC-MS/MS

Rela�ve Intensity

MALDI MS/MS Analysis m/z

Intensity

Treated

TMT10-128N

Mix

114

Grow Cells in Medium with Heavy Isotopes

Control

TMT10-127C

Mix

Proteins

TMT

8 Da

m/z

117

Intensity

m/z

NC

NC NC

NC

m/z

characteristics of itraq, tmt and silac Characteristics

iTRAQ

TMT

SILAC

Labeling Method

In vitro

In vitro

In vivo

Label Specifica�ons

4plex/8plex

Duplex/6plex/10plex

-

Repor�ng group molecular mass

113-121; The minimum molecular mass difference between labeled reagents was 1 Da

126-131; The minimum molecular mass difference between labeled reagents was 6/1000 Da

-

TOF and Orbitrap mass spectrometry

The mass spectrometer has a resolu�on of at least 50,000 to dis�nguish different tags. Older versions of obtrap instruments can only dis�nguish 6plex

TOF and Orbitrap mass spectrometry

High throughput High protein coverage Quan�ta�ve accuracy High credibility Data-rich

A. Labeling efficiency can be up to 100% B. Good quan�ta�ve repeatability, low protein consump�on C. Suitable for the iden�fica�on and quan�fica�on of membrane proteins D. Closer to the real state of the sample

Suitable mass spectrometer

Advantages

Disadvantages

High throughput High protein coverage Quan�ta�ve accuracy High credibility Data-rich

A. Sample prepara�on and enzyma�c processes may cause discrepancies between parallel samples, resul�ng in biased results. B. Occurrence of interference between co-screening and co-fragmenta�on of the precursor ion for complex samples.

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It is mainly suitable for passageable cells or bacteria. Other experimental materials are not applicable. Long turnaround �me


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