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10 EA
1620,00 zł
1620,00 zł
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Informacje o tej pozycji
UNSPSC Code:
12352200
NACRES:
NA.56
Przejdź do
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Ta pozycja | 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 MS 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. This product is ideal for rapid protein digestion of small volumes (100 μl or less). Eluted peptides are ready for MS analysis, and require no additional clean-up.
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. This product is ideal for rapid protein digestion of small volumes (100 μl or less). Eluted peptides are ready for MS analysis, and require no additional clean-up.
Features and Benefits
Discover the advantages for yourself!
- 15 minute digestion
- Ideal for 10 to 100 μg of protein sample
- Minimal chymotryptic activity
- No additional clean-up required
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Numer produktu
Opis
Cennik
signalword
Warning
hcodes
Hazard Classifications
Acute Tox. 4 Oral
Klasa składowania
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
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
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
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
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
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
Powiązane treści
High Density Immobilized Trypsin in a Spin Column Format for Rapid Proteolysis and Increased Sequence Coverage
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