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4 X 25 μG
$161.00
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$438.00
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biological source
bovine pancreas
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
1 of 4
This Item | |||
|---|---|---|---|
| biological source bovine pancreas | biological source bovine pancreas | biological source - | biological source - |
| specific activity ≥80 units/mg protein | specific activity - | specific activity ≥150 units/mg protein | specific activity ≥2.5 units/mg protein |
| 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.[1] 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.[2]
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.[3] 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.[3] Trypsin Sequencing Grade generates glycopeptides from purified glycoproteins and is suited for the digestion of proteins in polyacrylamide gels.
Biochem/physiol Actions
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%
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 in acid is necessary for stability of solution: 0.01% TFA (v/v), 1 mM HCl or 0.1% acetic acid are recommended.
Analysis Note
Purity: Free of impurities that may interfere with the separation of peptides in reversed-phase HPLC.
Other Notes
For life science research only. Not for use in diagnostic procedures.
signalword
Danger
hcodes
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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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
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
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
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