Ugrás a tartalomra
Merck

TRYPSEQ-RO

Roche

Trypsin Sequencing Grade

from bovine pancreas

Szinonimák:

trypsin

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

Enzyme Commission szám:
UNSPSC kód:
12352204

biológiai forrás

bovine pancreas

Minőségi szint

form

lyophilized (salt-free)

specifikus aktivitás

≥80 units/mg protein

molekulatömeg

Mr 23.5 kDa

kiszerelés

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

gyártó/kereskedő neve

Roche

optimális pH

8.0

tárolási hőmérséklet

2-8°C

Related Categories

Általános leírás

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.

Egyediség

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%

Alkalmazás

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.

Minőség

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

Elkészítési megjegyzés

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.

Feloldás

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

Egyéb megjegyzések

For life science research only. Not for use in diagnostic procedures.

Piktogramok

Exclamation markHealth hazard

Figyelmeztetés

Danger

Figyelmeztető mondatok

Veszélyességi osztályok

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

Célzott szervek

Respiratory system

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 1

Lobbanási pont (F)

does not flash

Lobbanási pont (C)

does not flash


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

Már rendelkezik ezzel a termékkel?

Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

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
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
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

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