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Citations & References (4)
Thermo Scientific™
TMT11-131C Label Reagent
Tandem mass tag (TMT) reagents are specially designed to enable identification and quantitation of proteins in different samples using tandem mass spectrometry.
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| Catalog Number | Quantity |
|---|---|
| A37725 | 3 x 0.8 mg (per tag) |
| A34807 | 1 x 5 mg |
| A37724 | 3 x 0.8 mg |
| A34808 | 1 x 5 mg (per tag) |
Catalog number A37725
Price (EUR)
3.630,00
Each
Quantity:
3 x 0.8 mg (per tag)
Price (EUR)
3.630,00
Each
Tandem mass tag (TMT) reagents are specially designed to enable identification and quantitation of proteins in different samples using tandem mass spectrometry. The TMT11-131C tag structure is identical to the other TMT10pex tags, but the TMT11-131C mass reporter is labeled with only 13C isotopes. The addition of the TMT11-131C tag enables separation of the 131-mass reporter ion of the original TMT10plex reagents into N and C variants, creating an 11th channel for relative quantitation using high resolution Orbitrap MS instruments.
The advantages of TMT label reagents include increased multiplexed relative quantitation, increased sample throughput, and fewer missing quantitative values among samples. TMT10plex label reagents plus TMT11-131C is ideal for analysis of multiple protein samples from inhibitor dose response experiments, time course experiments, or to improve statistics on biological replicates.
Features of this TMT11-131C Label Reagent include:
• Multiplex—concurrent MS analysis of up to 11 samples derived from cells, tissues, or biological fluids
• Robust—increased multiplex capability results in fewer missing quantitative values among samples and higher confidence among replicates
• 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 Orbirtrap MS/MS platforms, with data analysis fully supported by Proteome Discoverer 2.3
TMT11-131C is available as a standalone tag (Cat. No. A34807, A37724), as part of this TMT10plex Isobaric Label Reagent Set plus TMT11-131C, or as part of the complete 11plex set of reagents in a 96-well plate format. When combined with the industry-leading, high resolution Orbitrap instruments and software, TMT reagents provide integrated total solutions for quantitative protein expression analysis.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Final Product TypePeptide
For Use With (Equipment)Mass Spectrometer
Label or DyeMass Isotopes of Amino Acids
Quantity3 x 0.8 mg (per tag)
Shipping ConditionDry Ice
Workflow StepPeptide Labeling
Detection MethodMass Spectrometry
Product LineTMT10plex
Product TypeIsobaric Label Reagent
Starting MaterialPeptides
Unit SizeEach
Contents & Storage
3 sets of 11 vials, store at –5 to –30°C
Citations & References (4)
Citations & References
Abstract
Cell-type and subcellular compartment-specific APEX2 proximity labeling reveals activity-dependent nuclear proteome dynamics in the striatum.
Journal:Nature communications
PubMed ID:34381044
The vertebrate brain consists of diverse neuronal types, classified by distinct anatomy and function, along with divergent transcriptomes and proteomes. Defining the cell-type specific neuroproteomes is important for understanding the development and functional organization of neural circuits. This task remains challenging in complex tissue, due to suboptimal protein isolation techniques
Comparison of plastid proteomes points towards a higher plastidial redox turnover in vascular tissues than in mesophyll cells.
Journal:Journal of experimental botany
PubMed ID:37026385
Plastids are complex organelles that vary in size and function depending on the cell type. Accordingly, they can be referred to as amyloplasts, chloroplasts, chromoplasts, etioplasts, or proplasts, to only cite a few. Over the past decades, methods based on density gradients and differential centrifugation have been extensively used for
Correction: Biochemical characterization of protease activity of Nsp3 from SARS-CoV-2 and its inhibition by nanobodies
Journal:PLoS One
PubMed ID:38626090
[This corrects the article DOI: 10.1371/journal.pone.0253364.]. CI - Copyright: © 2024 Armstrong et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Decellularization alters the unfavorable regenerative adverse microenvironment of the injured spinal cord to support neurite outgrowth.
Journal:Annals of translational medicine
PubMed ID:36172103
BACKGROUND: Acellular tissue has been transplanted into the injury site as an external microenvironment to intervene with imbalance microenvironment that occurs after spinal cord injury (SCI) and stimulating axonal regeneration, although the mechanism is unclear. Given decellularization is the key means to obtain acellular tissues, we speculated changes in the