RTRYP-RO

Roche

Trypsin recombinant, Proteomics Grade

Name: Trypsin recombinant, Proteomics Grade
Brand: ROCHE

recombinant enzyme expressed in Pichia pastoris

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About This Item

EC Number:

3.4.21.4 (BRENDA, IUBMB)

NACRES:

NA.21

UNSPSC Code:

12352204

Specific activity:

≥150 units/mg protein

Assay:

95% (gel filtration)

Recombinant:

expressed in Pichia pastoris

Key Documents

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recombinant

expressed in Pichia pastoris

assay

95% (gel filtration)

form

lyophilized

specific activity

≥150 units/mg protein

packaging

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

manufacturer/tradename

Roche

storage temp.

−20°C

Related Categories

Proteases

Proteins & Enzymes

Roche Life Science Products

Tissue Dissociation

Labware Partners

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This Item	EMS0007	EMS0006	TRYPSEQM-RO
Roche RTRYP-RO Trypsin recombinant, Proteomics Grade	Sigma-Aldrich EMS0007 Recombinant Trypsin Dimethlyated	Sigma-Aldrich EMS0006 Recombinant Trypsin	Roche TRYPSEQM-RO Trypsin Sequencing Grade, modified
specific activity ≥150 units/mg protein	specific activity ≥10,000 units/mg protein	specific activity ≥10,000 units/mg protein	specific activity -
assay 95% (gel filtration)	assay -	assay -	assay -
form lyophilized	form lyophilized powder	form lyophilized powder	form lyophilized (salt-free)
recombinant expressed in Pichia pastoris	recombinant expressed in Pichia pastoris	recombinant expressed in Pichia pastoris	recombinant -
storage temp. −20°C	storage temp. 2-8°C	storage temp. 2-8°C	storage temp. 2-8°C
Quality Level 100	Quality Level 200	Quality Level 200	Quality Level 100

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.

Application

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.[1][2]

Biochem/physiol Actions

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.

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.

pictograms

GHS07,GHS08

signalword

Danger

hcodes

H315 - H319 - H334 - H335

pcodes

P261 - P264 - P280 - P284 - P304 + P340 + P312 - P342 + P311

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

does not flash

flash_point_c

does not flash

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Quantitative peptide and protein profiling by mass spectrometry.

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

Changes in tear protein profile in keratoconus disease.

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