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T7309

Trypsin from bovine pancreas

≥2,500 USP units/mg solid, meets USP testing specifications

Synonym(s):

Serine Protease 1

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Size/SKUAvailabilityPrice
1 g
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$568.00
10 g
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$3,400.00

About This Item

CAS Number:
9002-07-7
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-650-8
MDL number:
MFCD00082094
EC Number:
3.4.21.4 (BRENDA, IUBMB)
Specific activity:
≥2,500 USP units/mg solid

$568.00

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Quality Segment

300

agency

USP/NF, meets USP testing specifications

form

solid

specific activity

≥2,500 USP units/mg solid

mol wt

23.8 kDa

purified by

crystallization

solubility

H2O: soluble, saline: soluble

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

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.

Preparation Note

Soluble in 1 mM HCl at 1 mg/mL.

Other Notes

One BAEE unit will produce a A253 of 0.001 per minute at pH 7.6 at 25°C using BAEE as a substrate.
Trypsin consists of a single chain polypeptide of 223 amino acid residues, produced by the removal of the N-terminal hexapeptide from trypsinogen which is cleaved at the Lys - lle peptide bond. The sequence of amino acids is cross-linked by 6 disulfide bridges. This is the native form of trypsin, beta-trypsin. BETA-trypsin can be autolyzed, cleaving at the Lys - Ser residue, to produce alpha-trypsin. Trypsin is a member of the serine protease family.

Disclaimer

Solutions in 1 mM HCl are stable for 1 year in aliquots and stored at -20°C. The presence of Ca2+ will also diminish the self-autolysis of trypsin and maintain its stability in solution. Trypsin will also retain most of its activity in 2.0 M urea, 2.0 M guanidine HCl, or 0.1% (w/v) SDS.

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Trypsin from bovine pancreas ≥2,500 USP units/mg solid, meets USP testing specifications

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T7309

Trypsin from bovine pancreas

Trypsin from porcine pancreas Type IX-S, lyophilized powder, 13,000-20,000 BAEE units/mg protein

Sigma-Aldrich

T0303

Trypsin from porcine pancreas

Trypsin from porcine pancreas lyophilized powder, Type II-S, 1,000-2,000 units/mg dry solid

Sigma-Aldrich

T7409

Trypsin from porcine pancreas

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

Sigma-Aldrich

T8802

Trypsin from bovine pancreas

description

≥2,500 USP units/mg solid, meets USP testing specifications

description

Type IX-S, lyophilized powder, 13,000-20,000 BAEE units/mg protein

description

lyophilized powder, Type II-S, 1,000-2,000 units/mg dry solid

description

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

specific activity

≥2,500 USP units/mg solid

specific activity

13,000-20,000 BAEE units/mg protein

specific activity

1,000-2,000 units/mg dry solid

specific activity

≥10,000 BAEE units/mg protein

application(s)

diagnostic assay manufacturing

application(s)

diagnostic assay manufacturing

application(s)

-

application(s)

-

form

solid

form

lyophilized powder

form

lyophilized powder

form

essentially salt-free, lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

mol wt

23.8 kDa

mol wt

23.8 kDa

mol wt

23.8 kDa

mol wt

23.8 kDa

solubility

H2O: soluble, saline: soluble

solubility

-

solubility

-

solubility

hydrochloric acid: soluble 1 mM, clear

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pictograms

Health hazardExclamation mark
GHS08,GHS07

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

ppe

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

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