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93614 Sigma

Trypsin from porcine pancreas

≥10000 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,
form   powder
mol wt   mol wt 23.8 kDa
foreign activity   chymotrypsin ≤0.2%
shipped in   wet ice
storage temp.   −20°C

Description

Other Notes

Sales restrictions may apply

Used as a cell-detachment agent (Trypsinization of tissue fragments)

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 ΔA253 of 0.001 per min at pH 7.6 at 25° C using BAEE as substrate. One BTEE unit = 320 ATEE units. Reaction volume = 3.2 mL (1 cm light path).

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 digestionsns†. 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.

Price and Availability

Suggested Laboratory Gloves


Laboratory GlovesThis substance has been tested against several types of hand protection for CE compliance. Click below to find the recommended gloves for handling this product.



Safety & Documentation

Safety Information

Symbol 
Signal word 
Danger
Hazard statements 
Precautionary statements 
Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
1
RTECS 
YN5075000
Protocols & Articles

Protocols

Procedure for Enzymatic Assay of Trypsin (EC 3.4.21.4)

This procedure is for products with a specification for Trypsin activity using Nα-Benzoyl-L-arginine ethyl ester (BAEE) as a substrate. The procedure is a continuous spectrophotometric rate determina...

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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