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Citations & References (7)
Thermo Scientific™
Pierce™ Peptide Desalting Spin Columns
Pierce Peptide Desalting Spin Columns provide a convenient and reproducible way to desalt and remove contaminants from peptide samples prior to analysis by mass spectrometry.
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| Catalog Number | Quantity |
|---|---|
| 89851 | 50 Columns |
| 89852 | 25 Columns |
Catalog number 89851
Price (EUR)
480,00
Each
Quantity:
50 Columns
Price (EUR)
480,00
Each
Thermo Scientific Pierce Peptide Desalting Spin Columns are ready-to-use centrifuge spin columns that enable efficient desalting of peptide samples following enzymatic digestion. The polymer-based hydrophobic resin contained in each column provides excellent binding and recovery characteristics for peptide samples in preparation for mass spectrometry and other methods. Each spin column can bind from 5 μg to 5 mg of native and TMT-labeled peptides. The spin column format allows processing of multiple samples (10–300 μL each) in parallel in approximately 30 minutes.
Mass spectrometry is essential for studying biological compounds. However, many of the buffers and reagents used for sample preparation interfere with mass spectrometry analysis, leading to poor-quality spectra and reduced sensitivity. Pierce Peptide Desalting Spin Columns are designed to remove many of the interfering hydrophilic sample contaminants with minimal sample loss, thus enabling sensitive and comprehensive analysis of digested protein samples by mass spectrometry.
• Remove MS-interfering contaminants—significantly reduces signal suppression and improves sensitivity in mass spectrometry
• High binding capacity—hydrophobic polymer-based resin allows for recovery of peptide loads of native and TMT-labeled peptides from 5 μg to 5 mg
• Easy to use—resin is provided in single-use spin column format that fits common 2-mL tubes
• Compatible—resin is validated with a variety of complex samples, including TMT-labeled peptides, and is stable under extreme pH conditions
• Remove MS-interfering contaminants—significantly reduces signal suppression and improves sensitivity in mass spectrometry
• High binding capacity—hydrophobic polymer-based resin allows for recovery of peptide loads of native and TMT-labeled peptides from 5 μg to 5 mg
• Easy to use—resin is provided in single-use spin column format that fits common 2-mL tubes
• Compatible—resin is validated with a variety of complex samples, including TMT-labeled peptides, and is stable under extreme pH conditions
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Final Product TypePeptide
Quantity50 Columns
Shipping ConditionRoom Temperature
Detection MethodMass Spectrometry
FormatSpin Column
Product LinePierce
Product TypeSpin Desalting Column
Unit SizeEach
Contents & Storage
Store at 2–8°C.
Frequently asked questions (FAQs)
How do I determine if my sample is compatible and ready for LC-MS?
After TMT reagent labeling, I still see a lot of excess TMT tags in my sample. How should I remove it?
I'm seeing a peak in my mass spectrometry analysis results that seems to always be present in my system. What can I do?
I cleaned up my peptide sample using C18 or desalting columns, but I lost most of my peptides. What went wrong?
If I already removed small contaminants and detergents at the protein level, do I still need to desalt my peptides prior to mass spectrometry analysis?
Citations & References (7)
Citations & References
Abstract
PhoXplex: Combining Phospho-enrichable Cross-Linking with Isobaric Labeling for Quantitative Proteome-Wide Mapping of Protein Interfaces.
Journal:Journal of proteome research
PubMed ID:39422127
Integrating cross-linking mass spectrometry (XL-MS) into structural biology workflows provides valuable information about the spatial arrangement of amino acid stretches, which can guide elucidation of protein assembly architecture. Additionally, the combination of XL-MS with peptide quantitation techniques is a powerful approach to delineate protein interface dynamics across diverse conditions. While
Standard Flow Multiplexed Proteomics (SFloMPro)-An Accessible Alternative to NanoFlow Based Shotgun Proteomics.
Journal:Proteomes
PubMed ID:35076613
Multiplexed proteomics using isobaric tagging allows for simultaneously comparing the proteomes of multiple samples. In this technique, digested peptides from each sample are labeled with a chemical tag prior to pooling sample for LC-MS/MS with nanoflow chromatography (NanoLC). The isobaric nature of the tag prevents deconvolution of samples until fragmentation
Plasmodium falciparum Calcium-Dependent Protein Kinase 4 is Critical for Male Gametogenesis and Transmission to the Mosquito Vector.
Journal:mBio
PubMed ID:34724830
Gametocytes of the malaria parasite Plasmodium are taken up by the mosquito vector with an infectious blood meal, representing a critical stage for parasite transmission. Calcium-independent protein kinases (CDPKs) play key roles in calcium-mediated signaling across the complex life cycle of the parasite. We sought to understand their role in
Introducing Bacillus natto and Propionibacterium shermanii into soymilk fermentation: A promising strategy for quality improvement and bioactive peptide production during in vitro digestion.
Journal:Food chemistry
PubMed ID:38850988
Herein, the texture properties, polyphenol contents, and in vitro protein digestion characteristics of soymilk single- or co-fermented by non-typical milk fermenter Bacillus natto (B. natto), Propionibacterium freudenreichii subsp. shermanii (P. shermanii), and traditional milk fermenter were evaluated. Co-fermenting procedure containing B. natto or P. shermanii could raise the amounts of
Cryo-EM structure of the KLHL22 E3 ligase bound to an oligomeric metabolic enzyme.
Journal:Structure (London, England : 1993)
PubMed ID:37788672
CULLIN-RING ligases constitute the largest group of E3 ubiquitin ligases. While some CULLIN family members recruit adapters before engaging further with different substrate receptors, homo-dimeric BTB-Kelch family proteins combine adapter and substrate receptor into a single polypeptide for the CULLIN3 family. However, the entire structural assembly and molecular details have