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T7168

Trypsin from porcine pancreas

tablet, 1 mg tablet

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20 tabs

Available to ship TODAYfromMILWAUKEE

$59.20
50 tabs

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$108.00

About This Item

CAS Number:
9002-07-7
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
3.4.21.4 (BRENDA, IUBMB)
MDL number:
MFCD00082094
Specific activity:
90-110% (compared to standard)
Biological source:
Porcine pancreas

$59.20

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biological source

Porcine pancreas

Quality Segment

form

tablet

specific activity

90-110% (compared to standard)

mol wt

23.8 kDa

storage temp.

−20°C

General description

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.

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.
For use in immunohistochemical procedures to enhance staining and to unmask antigens after routine fixation and processing.

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

This product is a lyophilized powder soluble in Hank′s Balanced Salt Solution at 25 mg/mL.
For applications that require EDTA, solubilizing trypsin should be done with a buffered salt solution contaiing no Ca2+ or Mg2+.

Other Notes

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).

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 porcine pancreas tablet, 1 mg tablet

Sigma-Aldrich

T7168

Trypsin from porcine pancreas

Trypsin from porcine pancreas lyophilized powder, BioReagent, suitable for cell culture, 1,000-2,000 BAEE units/mg solid

Sigma-Aldrich

T4799

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Sigma-Aldrich

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T4424

Trypsin solution 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

description

tablet, 1 mg tablet

description

lyophilized powder, BioReagent, suitable for cell culture, 1,000-2,000 BAEE units/mg solid

description

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

description

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

specific activity

90-110% (compared to standard)

specific activity

1,000-2,000 BAEE units/mg solid

specific activity

-

specific activity

1,000-2,000 units/mg dry solid

biological source

Porcine pancreas

biological source

Porcine pancreas

biological source

Porcine pancreas

biological source

-

form

tablet

form

lyophilized powder

form

solution

form

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

23.4 kDa

mol wt

23.8 kDa

Quality Level

200

Quality Level

200

Quality Level

400

Quality Level

200

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Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Codes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

PPE (personal protective equipment)

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

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