Thermo Scientific™

TMTduplex™ Isobaric Label Reagent Set, 5 x 0.8 mg

Catalog number: 90065
Thermo Scientific™

TMTduplex™ Isobaric Label Reagent Set, 5 x 0.8 mg

Catalog number: 90065
Catalog Number
90065
Unit Size
5 x 0.8 mg (per tag)
Price (USD)
Price: 798.00
Your Price:
Availability
-
Quantity
Catalog NumberUnit SizePrice (USD)AvailabilityQuantity
900655 x 0.8 mg (per tag)
Price: 798.00
Your Price:
-
Product Overview
Figures
Videos
Recommendations
Recommendations
Documents
FAQ
Citations & References
Additional Information
Recommendations

Tandem Mass Tag™ 2-plex (TMTduplex™) Isotopic Label Reagents comprise “light” TMTzero and “heavy” TMT6-127 label reagents while Tandem Mass Tag™ 2-plex (TMTduplex) Isobaric Label Reagents comprise “heavy” TMT2-126 and TMT2-127 Label Reagents for multiplexing. Both sets of label reagents have the same structure that are NHS-activated for covalent, irreversible labeling of primary amine groups (—NH2).

Tandem Mass Tag (TMT) Reagents are chemical tags that enable identification and quantitation of proteins in different samples using tandem mass spectrometry. The amine-reactive, NHS-ester-activated compounds covalently attach to the peptide amino terminus and free amino termini of lysine residues of peptides and proteins with high efficiency, thereby labeling all peptides in each sample regardless of enzyme used for digestion.

During MS/MS analysis, each TMT tag is also fragmented to produce a unique reporter ion mass that is used for sample identification and quantitation. Protein quantitation is accomplished by comparing the relative intensities of the two reporter ions in the MS/MS spectra. Our TMTduplex reagents label all peptides for analysis of two samples in a single MS analysis.

Features of TMTduplex Isobaric and Isotopic Label Reagent Sets:
Powerful—concurrent MS analysis of two samples increases throughput and enables relative quantitation of two different treatment conditions (up to 5 experiments per set)
Consistent—identical reagent structure and performance among TMTzero, TMTduplex, TMTsixplex and TMT10plex reagents allows efficient transition from method development to multiplex quantitation, enabling biomarker discovery research across platforms and data sets
Robust—consistent chemistry allows efficient transition from method development to multiplex quantitation
Efficient—amine-reactive NHS-ester activated reagents ensure efficient labeling of all peptides regardless of protein sequence or proteolytic enzyme specificity
Compatible—optimized for use with high resolution Thermo Scientific Orbitrap MS/MS platforms, with data analysis fully supported by Proteome Discoverer™ 2.4 and above

Applications:
• Protein expression profiling of normal vs. disease states or control vs. treated
• Measurement of two different samples concurrently in a single experiment
• Quantitative analysis of proteins for which no antibodies are available
• dentification and quantitation of membrane and post-translationally modified proteins
• Identification and quantitation of hundreds to thousands of proteins in a single experiment

TMT Reagents are provided as standalone sets or in optimized kit formats containing all necessary reagents and controls for maximum flexibility, convenience and reliability. Tandem Mass Tag Reagents combined with the industry leading instruments and software provide integrated total system solutions for quantitative protein expression analysis.

For Research Use Only. Not for use in diagnostic procedures.

Specifications

Description
TMTduplex™ Isobaric Label Reagent Set, 5 x 0.8 mg
For Use With (Equipment)
Mass Spectrometer
Product Line
TMTduplex™
Starting Material
Cell Lysate
Final Product Type
Protein
Detection Method
Mass Spectrometry
Workflow Step
Protein Labeling
Quantity
5 x 0.8 mg (per tag)

Contents & Storage

Sufficient for: Five duplex (5 x 2-way) experiments
• TMT2-126 Label Reagent, 5 x 0.8 mg
• TMT2-127 Label Reagent, 5 x 0.8 mg

Store at –20°C.

Figures

Documents & Downloads

Certificates

    Frequently asked questions (FAQs)

    Citations & References

    Search citations by name, author, journal title or abstract text