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TRYPSEQ-RO

Roche

Trypsin Sequencing Grade

from bovine pancreas

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Synonym(s):
trypsin
Enzyme Commission number:

biological source

bovine pancreas

Quality Level

form

lyophilized (salt-free)

specific activity

≥80 units/mg protein

mol wt

Mr 23.5 kDa

packaging

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

manufacturer/tradename

Roche

optimum pH

8.0

storage temp.

2-8°C

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This Item
TRYPSEQM-RORTRYP-RO650275
Trypsin Sequencing Grade from bovine pancreas

TRYPSEQ-RO

Trypsin Sequencing Grade

biological source

bovine pancreas

biological source

bovine pancreas

biological source

-

biological source

-

form

lyophilized (salt-free)

form

lyophilized (salt-free)

form

lyophilized

form

lyophilized solid

mol wt

Mr 23.5 kDa

mol wt

24.000 g/mol

mol wt

-

mol wt

-

optimum pH

8.0

optimum pH

8.0

optimum pH

-

optimum pH

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

General description

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.

Specificity

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%

Application

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.

Quality

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

Preparation Note

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.

Reconstitution

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

Other Notes

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

Pictograms

Exclamation markHealth hazard

Signal Word

Danger

Hazard Statements

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

does not flash

Flash Point(C)

does not flash


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