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TRYPSEQM-RO

Roche

Trypsin Sequencing Grade, modified

from bovine pancreas

Synonim(y):

Trypsin

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About This Item

Numer EC enzymu:
Kod UNSPSC:
12352204

pochodzenie biologiczne

bovine pancreas

Poziom jakości

klasa czystości

protein sequencing grade

Postać

lyophilized (salt-free)

masa cząsteczkowa

24.000 g/mol

opakowanie

pkg of 4 × 100 μg (11418033001)
pkg of 4 × 25 μg (11418025001)

producent / nazwa handlowa

Roche

warunki przechowywania

(Keep container tightly closed in a dry and well-ventilated place.)

stężenie

0.01-0.2 % (w/w)

metody

protein sequencing: suitable

zanieczyszczenia

Chymotrypsin

kolor

white

optymalne pH

8.0

rozpuszczalność

10 g/L

przydatność

suitable for protein modification

numer dostępu UniProt

Zastosowanie

life science and biopharma

obecność zanieczyszczeń

Contaminating activities corresponds
Chymotrypsin , contains

temp. przechowywania

2-8°C

informacje o genach

Opis ogólny

Trypsin Sequencing Grade, modified, is isolated from bovine pancreas as a highly purified and specific protease, and subsequently modified.

Trypsin is a highly efficient and specific protease widely used in proteomics for protein digestion. It produces short peptides with specific characteristics that are compatible with current separation and identification methods such as liquid chromatography, mass spectrometry (MS).

Inhibitors:
TLCK, DFP, PMSF, leupeptin, soybean trypsin inhibitor, trypsin inhibitor from hen egg, aprotinin, α2-macroglobulin,α1-antitrypsin, APMSF, and antipain.

Specyficzność

Trypsin is a serine endopeptidase. At pH 7.5–9, it specifically hydrolyzes proteins and peptide bonds C-terminally of Iysine and arginine. Amide and ester bonds of Arg and Lys are also cleaved. The specificity of Trypsin Sequencing Grade, modified, is verified with the oxidized B-chain of insulin (insulin Box) as a substrate. High concentrations of Trypsin Sequencing Grade, modified, one part by weight enzyme with 9 parts by weight insulin Box, are incubated for 18 hours to detect traces ofchymotrypsin impurities.

Zastosowanie

Use Trypsin Sequencing Grade, modified, to generate glycopeptides from purified glycoproteins.
It is used for:
  • Protein-structure elucidation
  • Tryptic mapping
  • Fingerprinting analysis
  • Sequence analysis
  • Translocation studies
  • Protein identification
  • Protein digestion during lipoprotein preparation for liquid chromatography-tandem mass spectrometry (LC-MS/MS)

Jakość

Purity: Free of impurities that may interfere with the separation of peptides in reversed-phase HPLC.

Uwaga dotycząca przygotowania

Working concentration: 1/100 to 1/5 of the protein by weight
Storage conditions (working solution): -15 to -25 °C
Trypsin Sequencing Grade, modified, is more resistant to autolysis, even at pH values in the neutral and weakly basic range. The enzyme can be used in high concentrations.
A solution in 1% acetic acid or 1 mM HCI can be used for up to one week when stored at 2 to 8° C. Stored in aliquots at -15 to -25 °C, the solution is stable for at least one year without loss of activity.

Przechowywanie i stabilność

Store dry

Inne uwagi

For life science research only. Not for use in diagnostic procedures.
This page may contain text that has been machine translated.

Piktogramy

Exclamation markHealth hazard

Hasło ostrzegawcze

Danger

Zwroty wskazujące rodzaj zagrożenia

Zwroty wskazujące środki ostrożności

Klasyfikacja zagrożeń

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Organy docelowe

Respiratory system

Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 1

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

Poszukaj Certyfikaty analizy (CoA), wpisując numer partii/serii produktów. Numery serii i partii można znaleźć na etykiecie produktu po słowach „seria” lub „partia”.

Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Scott J Walmsley et al.
Journal of proteome research, 12(12), 5666-5680 (2013-10-15)
Trypsin is an endoprotease commonly used for sample preparation in proteomics experiments. Importantly, protein digestion is dependent on multiple factors, including the trypsin origin and digestion conditions. In-depth characterization of trypsin activity could lead to improved reliability of peptide detection
Desalegn Begna et al.
Journal of proteome research, 10(9), 4263-4280 (2011-07-15)
Despite their similar genetic makeup, honeybee (A. mellifera) queens and workers show alternative morphologies driven by nutritional difference during the larval stage. Although much research have been done to investigate the causes of honeybee caste polymorphism, information at subcellular protein
Xuchu Wang et al.
Molecular & cellular proteomics : MCP, 12(8), 2174-2195 (2013-05-11)
Thellungiella halophila, a close relative of Arabidopsis, is a model halophyte used to study plant salt tolerance. The proteomic/physiological/transcriptomic analyses of Thellungiella plant leaves subjected to different salinity levels, reported herein, indicate an extraordinary ability of Thellungiella to adapt to
Jianke Li et al.
PloS one, 5(10), e13455-e13455 (2010-10-27)
Honeybee (Apis mellifera) exhibits divisions in both morphology and reproduction. The queen is larger in size and fully developed sexually, while the worker bees are smaller in size and nearly infertile. To better understand the specific time and underlying molecular
Samuel Ogden et al.
NAR cancer, 5(1), zcad001-zcad001 (2023-01-26)
Oesophageal adenocarcinoma (OAC) is a deadly disease with poor survival statistics and few targeted therapies available. One of the most common molecular aberrations in OAC is amplification or activation of the gene encoding the receptor tyrosine kinase ERBB2, and ERBB2

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