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T8802

Sigma-Aldrich

Trypsin from bovine pancreas

TPCK Treated, essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein

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CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

biological source

bovine pancreas

Quality Level

sterility

aseptically filled

form

essentially salt-free, lyophilized powder

specific activity

≥10,000 BAEE units/mg protein

mol wt

23.8 kDa

composition

protein, ≥95%

solubility

hydrochloric acid: soluble 1 mM, clear

foreign activity

Chymotrypsin ≤0.1 BTEE units/mg protein

storage temp.

−20°C

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This Item
T6424T1426T7168
Trypsin from bovine pancreas TPCK Treated, essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein

T8802

Trypsin from bovine pancreas

Sigma-Aldrich

T6424

Trypsin from human pancreas

Trypsin from bovine pancreas TPCK Treated, essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein

T1426

Trypsin from bovine pancreas

Trypsin from porcine pancreas tablet, 1 mg tablet

T7168

Trypsin from porcine pancreas

specific activity

≥10,000 BAEE units/mg protein

specific activity

-

specific activity

≥10,000 BAEE units/mg protein

specific activity

90-110% (compared to standard)

form

essentially salt-free, lyophilized powder

form

salt-free, lyophilized powder

form

essentially salt-free, lyophilized powder

form

tablet

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

mol wt

23.8 kDa

mol wt

-

mol wt

23.8 kDa

mol wt

23.8 kDa

sterility

aseptically filled

sterility

-

sterility

-

sterility

-

General description

The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.

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.
Trypsin can be used to release adherent cells from tissue culture plates for passaging. Trypsin has been used in a study to assess the effects of macromolecular crowding on the structural stability of human α-lactalbumin. Trypsin has also been used in a study to investigate BN-PAGE analysis of Trichoderma harzianum secretome.

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.

Unit Definition

One BAEE unit will produce a ΔA253 of 0.001 per min at pH 7.6 at 25 °C using BAEE as substrate. Reaction volume = 3.2 ml (1 cm light path).
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

TPCK treated

Analysis Note

Protein determined by E1%/280

Other Notes

View more information on trypsin at www.sigma-aldrich.com/enzymeexplorer

pictograms

Exclamation markHealth hazard

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


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Journal of proteome research, 14(2), 1308-1314 (2014-12-17)
Nonenzymatic deamidation occurs readily under the condition of trypsin digestion, resulting in the identification of many artificial deamidation sites. To evaluate the effect of trypsin digestion buffers on artificial deamidation, we compared the three commonly used buffers Tris-HCl (pH 8)
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Acta biochimica et biophysica Sinica, 44(8), 703-711 (2012-06-28)
The folding of protein, an important process for protein to fulfill normal functions, takes place in crowded physiological environments. α-Lactalbumin, as a model system for protein-folding studies, has been used extensively because it can form stable molten globule states under
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Protocols

Continuous spectrophotometric rate determination method using BAEE substrate measures trypsin activity, essential for enzyme characterization.

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