TRYPSEQ-RO
Roche
Trypsin Sequencing Grade
from bovine pancreas
Synonym(s):
trypsin
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About This Item
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
Related Categories
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%
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.
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.
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.
Signal Word
Danger
Hazard Statements
Precautionary 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
Regulatory Information
动植物源性产品
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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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