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Trypsin recombinant, Proteomics Grade

recombinant enzyme expressed in Pichia pastoris

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Enzyme Commission number:


expressed in Pichia pastoris

Quality Level


95% (gel filtration)



specific activity

≥150 units/mg protein


pkg of 4 × 100 μg (03708969001)
pkg of 4 × 25 μg (03708985001)



storage temp.


General description

This trypsin preparation is generated from the recombinant Pichia pastoris strain and is, thus, free of chymotrypsin. Trypsin recombinant, Proteomics Grade, exhibits high specific activity.


Serine endopeptidase, hydrolyzing specifically proteins and peptides at the carboxy side of the basic amino acids Arg and Lys. Amide and ester bonds of Arg and Lys are also cleaved.


Trypsin recombinant, Proteomics Grade, is used to specifically digest proteins separated by 2D gel electrophoresis or liquid chromatographic methods during sample preparation for mass spectrometry.

Preparation Note

Stabilizers: Ca2+ in mM concentration range
Inhibitors: TLCK, DFP, PMSF, leupeptin, soybean trypsin inhibitor, trypsin inhibitor from hen egg, aprotinin, α2-macroglobulin, α1-antitrypsin, APMSF, and antipain.
Storage conditions (working solution): -15 to -25°C
The reconstituted solution is stable for 1 month at -15 to -25°C. Avoid repeated freezing/thawing!


Following reconstitution in 10 mM HCl, Trypsin, recombinant, proteomics grade is stable at -15 to -25 °C for up to one month. After first reconstitution the product must be stored in appropriate aliquots to avoid repeated freezing and thawing.

Other Notes

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


Exclamation markHealth hazard



Hazard Classifications

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


Respiratory system

Storage Class

11 - Combustible Solids




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Alexander Schmidt et al.
Methods in molecular biology (Clifton, N.J.), 492, 21-38 (2009-02-26)
Proteomics may be defined as the systematic analysis of proteins expressed in a given organism (Electrophoresis 16:1090-1094, 1995). Important technical innovations in mass spectrometry (MS), protein identification methods, and database annotation, over the past decade, now make it possible to
A Acera et al.
Eye (London, England), 25(9), 1225-1233 (2011-06-28)
To analyze tear protein profile variations in patients with keratoconus (KC) and to compare them with those of control subjects. Tears from 12 normal subjects and 12 patients with KC were analyzed by two-dimensional gel electrophoresis (2-DE) and liquid chromatography-mass

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