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T4424

Sigma-Aldrich

Trypsin solution from porcine pancreas

1 ×, sterile-filtered, BioReagent, suitable for cell culture, 2.5 g porcine trypsin per liter in Hanks′ Balanced Salt Solution with phenol red

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

biological source

Porcine pancreas

Quality Level

sterility

sterile-filtered

product line

BioReagent

form

solution

mol wt

23.4 kDa

concentration

1 ×

technique(s)

cell culture | mammalian: suitable

impurities

Porcine parvovirus, none detected (9 CFR)

pH

7.0-7.6

shipped in

dry ice

storage temp.

−20°C

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1 of 4

This Item
T4674T4549T5266
vibrant-m

T5266

Trypsin from porcine pancreas

biological source

Porcine pancreas

biological source

Porcine pancreas

biological source

Porcine

biological source

Porcine pancreas

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

pH

7.0-7.6

pH

7.6

pH

7.6

pH

-

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

shipped in

wet ice

Application

Trypsin solution from porcine pancreas has been used for keratinocyte isolation and staining. It has also been used as a component of CMF-Steinberg′s solution to replace heart tissues after centrifugation in a study to culture embryonic cardiomyocytes from Mexican axolotl.

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 a 2.5 g/L porcine trypsin solution in Hank′s Balanced Salt Solution with phenol red.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

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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