TT0010
Trypsin-Spinsäulen
Utilizes TPCK-treated porcine trypsin immobilized on a 20 µm silica support, ensuring minimal chymotryptic activity, suitable for mass spectrometry
Synonym(e):
Immobilized TPCK- treated Trypsin, Immobilized Trypsin
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10 EA
€ 362,00
€ 362,00
Versand innerhalb von 2 Wochen. (Bei Bestellungen außerhalb der USA rechnen Sie bitte zusätzlich 1-2 Wochen für die Lieferung ein)
Über diesen Artikel
UNSPSC Code:
12352200
NACRES:
NA.56
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Dieser Artikel | T7575 | PP0100 | EMS0005 |
|---|---|---|---|
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C |
| grade for proteomics | grade Proteomics Grade | grade - | grade Proteomics Grade |
General description
Enjoy all of the advantages of Proteomics Grade Trypsin in a 15-minute digestion. A staple of mass spec sample preparation, efficient tryptic digestion is essential to successful proteomic analyses. While traditional digests require up to 18 hours, the same digest can be accomplished in only 15 minutes using the Trypsin Spin Column, Proteomics Grade.
This ultra-micro spin column contains highly purified, TPCK-treated porcine trypsin immobilized on a spherical 20 micron silica support, chemically modified to minimize non-specific adsorption. Eluted peptides are ready for MS analysis, and require no additional clean-up. Ideal for rapid protein digestion of small volumes (100 μl or less), the Trypsin Spin Column is a New Spin on MS Sample Prep!
This ultra-micro spin column contains highly purified, TPCK-treated porcine trypsin immobilized on a spherical 20 micron silica support, chemically modified to minimize non-specific adsorption. Eluted peptides are ready for MS analysis, and require no additional clean-up. Ideal for rapid protein digestion of small volumes (100 μl or less), the Trypsin Spin Column is a New Spin on MS Sample Prep!
Features and Benefits
Entdecken Sie die Vorteile für sich selbst!
- 15 Minuten Verdau
- Ideal für 10 bis 100 μg Proteinproben
- Minimale chymotryptische Aktivität
- Keine zusätzliche Aufreinigung erforderlich
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Hazard Classifications
Acute Tox. 4 Oral
Lagerklasse
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
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Jiangjiang Liu et al.
Journal of the American Society for Mass Spectrometry, 20(5), 819-828 (2009-02-10)
This work uses electrospray ionization mass spectrometry (ESI-MS) in conjunction with hydrogen/deuterium exchange (HDX) and optical spectroscopy for characterizing the solution-phase properties of cytochrome c (cyt c) after heat exposure. Previous work demonstrated that heating results in irreversible denaturation for
Shama P Mirza et al.
Journal of proteome research, 7(7), 3042-3048 (2008-05-31)
Proteomics-based quantification methods for differential protein expression measurements are among the most important and challenging techniques in the field of mass spectrometry. Though numerous quantification methods have been established, no method meets all the demands for measuring accurate protein expression
Tomoharu Takeuchi et al.
Biological & pharmaceutical bulletin, 34(7), 1139-1142 (2011-07-02)
To study the endogenous counterpart of LEC-6, a major galectin in Caenorhabditis elegans, the proteomic analysis of glycoproteins captured by an immobilized LEC-6 column was performed using the nano liquid chromatography-tandem mass spectrometry (LC-MS/MS) technique. A protein recovered in a
Logan J Everett et al.
Journal of proteome research, 9(2), 700-707 (2009-12-02)
"Multi-stage" search strategies have become widely accepted for peptide identification and are implemented in a number of available software packages. We describe limitations of these strategies for validation and decoy-based statistical analyses and demonstrate these limitations using a set of
Julianne Backiel et al.
Biochemistry, 47(43), 11273-11284 (2008-10-04)
Enzymes of the Rnf family are believed to be bacterial redox-driven ion pumps, coupling an oxidoreduction process to the translocation of Na+ across the cell membrane. Here we show for the first time that Rnf is a flavoprotein, with FMN
Verwandter Inhalt
High Density Immobilized Trypsin in a Spin Column Format for Rapid Proteolysis and Increased Sequence Coverage
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