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T4549

Sigma-Aldrich

Trypsin solution from porcine pancreas

sterile-filtered, BioReagent, suitable for cell culture, 25 g porcine trypsin per liter in 0.9% sodium chloride

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CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.75

biological source

Porcine

Quality Level

sterility

sterile-filtered

product line

BioReagent

form

solution

mol wt

23.4 kDa

technique(s)

cell culture | mammalian: suitable

pH

7.6

shipped in

dry ice

storage temp.

−20°C

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This Item
T4674T4424T4799
sterility

sterile-filtered

sterility

sterile-filtered

sterility

sterile-filtered

sterility

-

form

solution

form

solution

form

solution

form

lyophilized powder

mol wt

23.4 kDa

mol wt

23.4 kDa

mol wt

23.4 kDa

mol wt

23.8 kDa

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable, single cell analysis: suitable

pH

7.6

pH

7.6

pH

7.0-7.6

pH

7.6

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.

Caution

This product should be stored frozen at -20°C.

Unit Definition

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

Preparation Note

This is 25 g/L porcine trypsin solution in 0.9% sodium chloride.

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

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Protocols

Trypsin is commonly used for dissociating adherent cells from surfaces. A wide variety of trypsin solutions are available to meet your specific cell line requirements.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

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