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93610 Sigma

Trypsin from bovine pancreas

essentially salt free, lyophilized, ~9000 U/mg

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Properties

Related Categories 3.4.x.x Peptidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Enzyme Class Index,
quality   essentially salt free
  lyophilized
mol wt   Mr ~23000
  mol wt 23.8 kDa
foreign activity   chymotrypsin ≤0.2%
shipped in   wet ice
storage temp.   −20°C

Description

Other Notes

Specifically hydrolyzes peptides, amides and esters at lysine and arginine carboxyl bonds ; Application in (selective) hydrolysis/condensation of carboxylic ester bonds

Unit Definition

1 U corresponds to the amount of enzyme which increases the absorbance at 253 nm by 0.001 per minute at pH 7.6 and 25°C (N-benzoyl-L-arginine ethyl ester, Cat. No. 12880, as substrate)

One BAEE unit will produce a A253 of 0.001 per minute at pH 7.6 at 25°C using BAEE as a substrate. One BTEE unit = 320 ATEE units

Application

For trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide. The typical use for this product is in removing adherent cells from a culture surface. The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture. Trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestions. Additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps.

Biochem/physiol Actions

Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues. The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. The optimal pH for trypsin activity is 7-9. Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. Removing these ions increases the enzymatic activity.

Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin.

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Safety Information

Symbol 
Signal word 
Danger
Hazard statements 
Precautionary statements 
Personal Protective Equipment 
WGK Germany 
1
RTECS 
YN5075000

Documents

Certificate of Analysis

Protocols & Articles

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

References

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