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TRYPSEQ-RO

Roche

Trypsin Sequencing Grade

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

Postać

lyophilized (salt-free)

aktywność właściwa

≥80 units/mg protein

masa cząsteczkowa

Mr 23.5 kDa

opakowanie

pkg of 4 × 100 μg (11047841001)
pkg of 4 × 25 μg (11418475001)

producent / nazwa handlowa

Roche

optymalne pH

8.0

temp. przechowywania

2-8°C

Powiązane kategorie

Opis ogólny

Trypsin Sequencing Grade is isolated from bovine pancreas as a highly purified and specific protease. Trypsin Sequencing Grade is a serine endopeptidase. It specifically cleaves peptide bonds at the carboxylic side of the basic amino acids Arg and Lys. Amide and ester bonds of Arg and Lys are also cleaved.

Specyficzność

The specificity of Trypsin Sequencing Grade is verified with the oxidized B-chain of insulin (insulin Box) as substrate. High concentrations of Trypsin Sequencing Grade (1 part by weight enzyme with 18 parts by weight insulin Box) are incubated for 18 hours to detect traces of chymotrypsin impurities.

Specificity (HPLC, with Insulin Box):
Cleavage after 1 hour: ≥90%;
Unspecific cleavage products after 18 hours: ≤10%

Zastosowanie

Trypsin Sequencing Grade is used to to digest proteins in solution, in gels or on blotting membranes.
The enzyme is used for protein-structure elucidation, tryptic mapping, fingerprinting, sequence analysis, and translocation studies. Trypsin Sequencing Grade generates glycopeptides from purified glycoproteins and is suited for the digestion of proteins in polyacrylamide gels.

Jakość

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

Uwaga dotycząca przygotowania

Stabilizers: Trypsin is stable in 4 M.
Working concentration: 1/100 to 1/20 of the protein by weight (in solution); 1-5 μg/100 μl (for in-gel digest)
Storage conditions (working solution): A solution in 0.01% trifluoroacetic acid (TFA), (v/v) or 1 mM HCl may be used for one week at maximum, if stored at 2 to 8 °C. By incubation of proteins in solution at neutral to slightly basic pH-values partial autolysis might occur. For this application, Roche recommends Trypsin, Modified, Sequencing Grade.

Rekonstytucja

Reconstitution in acid is necessary for stability of solution: 0.01% TFA (v/v), 1 mM HCl or 0.1% acetic acid are recommended.

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)

does not flash

Temperatura zapłonu (°C)

does not flash


Certyfikaty analizy (CoA)

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

Odwiedź Bibliotekę dokumentów

Saeedreza Vessal et al.
Journal of proteome research, 11(8), 4289-4307 (2012-07-07)
Protein expression patterns in imbibed seeds of three cultivars of chickpea (Cicer arietinum L.) with different rates of germination under limiting water supply in soil (>10% water holding capacity) were compared. A large number of soluble proteins expressed earlier and
Jesper V Olsen et al.
Molecular & cellular proteomics : MCP, 3(6), 608-614 (2004-03-23)
Almost all large-scale projects in mass spectrometry-based proteomics use trypsin to convert protein mixtures into more readily analyzable peptide populations. When searching peptide fragmentation spectra against sequence databases, potentially matching peptide sequences can be required to conform to tryptic specificity
Petra A Neff et al.
Chemphyschem : a European journal of chemical physics and physical chemistry, 8(14), 2133-2137 (2007-08-28)
A silicon-on-insulator (SOI) based thin film resistor is employed for the label-free determination of enzymatic activity. We demonstrate that enzymes, which cleave biological polyelectrolyte substrates, can be detected by the sensor. As an application, we consider the serine endopeptidase trypsin

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