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TRYPSEQM-RO

Roche

Trypsin Sequencing Grade, modified

from bovine pancreas

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Synonym(s):
Trypsin
Enzyme Commission number:

biological source

bovine pancreas

Quality Level

grade

protein sequencing grade

form

lyophilized (salt-free)

mol wt

24.000 g/mol

packaging

pkg of 4 × 100 μg (11418033001)
pkg of 4 × 25 μg (11418025001)

manufacturer/tradename

Roche

storage condition

(Keep container tightly closed in a dry and well-ventilated place.)

concentration

0.01-0.2 % (w/w)

technique(s)

protein sequencing: suitable

impurities

Chymotrypsin

color

white

optimum pH

8.0

solubility

10 g/L

suitability

suitable for protein modification

UniProt accession no.

application(s)

life science and biopharma

foreign activity

Contaminating activities corresponds
Chymotrypsin , contains

storage temp.

2-8°C

Gene Information

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This Item
TRYPSEQ-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

-

technique(s)

protein sequencing: suitable

technique(s)

-

technique(s)

-

technique(s)

-

Gene Information

cow ... PRSS1(780933)

Gene Information

-

Gene Information

-

Gene Information

-

form

lyophilized (salt-free)

form

lyophilized (salt-free)

form

lyophilized

form

lyophilized solid

suitability

suitable for protein modification

suitability

-

suitability

-

suitability

-

General description

Trypsin Sequencing Grade, modified, is isolated from bovine pancreas as a highly purified and specific protease, and subsequently modified.

Trypsin is a highly efficient and specific protease widely used in proteomics for protein digestion. It produces short peptides with specific characteristics that are compatible with current separation and identification methods such as liquid chromatography, mass spectrometry (MS).

Inhibitors:
TLCK, DFP, PMSF, leupeptin, soybean trypsin inhibitor, trypsin inhibitor from hen egg, aprotinin, α2-macroglobulin,α1-antitrypsin, APMSF, and antipain.

Specificity

Trypsin is a serine endopeptidase. At pH 7.5–9, it specifically hydrolyzes proteins and peptide bonds C-terminally of Iysine and arginine. Amide and ester bonds of Arg and Lys are also cleaved. The specificity of Trypsin Sequencing Grade, modified, is verified with the oxidized B-chain of insulin (insulin Box) as a substrate. High concentrations of Trypsin Sequencing Grade, modified, one part by weight enzyme with 9 parts by weight insulin Box, are incubated for 18 hours to detect traces ofchymotrypsin impurities.

Application

Use Trypsin Sequencing Grade, modified, to generate glycopeptides from purified glycoproteins.
It is used for:
  • Protein-structure elucidation
  • Tryptic mapping
  • Fingerprinting analysis
  • Sequence analysis
  • Translocation studies
  • Protein identification
  • Protein digestion during lipoprotein preparation for liquid chromatography-tandem mass spectrometry (LC-MS/MS)

Quality

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

Preparation Note

Working concentration: 1/100 to 1/5 of the protein by weight
Storage conditions (working solution): -15 to -25 °C
Trypsin Sequencing Grade, modified, is more resistant to autolysis, even at pH values in the neutral and weakly basic range. The enzyme can be used in high concentrations.
A solution in 1% acetic acid or 1 mM HCI can be used for up to one week when stored at 2 to 8° C. Stored in aliquots at -15 to -25 °C, the solution is stable for at least one year without loss of activity.

Storage and Stability

Store dry

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)

Not applicable

Flash Point(C)

Not applicable


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