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T4424

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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100 mL
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CHF 31.60
500 mL
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CHF 52.50

About This Item

CAS Number:
9002-07-7
EC Number:
3.4.21.4 (BRENDA, IUBMB)
UNSPSC Code:
12352204
NACRES:
NA.75
MDL number:
MFCD00082094
Biological source:
Porcine pancreas
Concentration:
1 ×

CHF 31.60

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biological source

Porcine pancreas

Quality Segment

400

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

Application

Trypsin solution from porcine pancreas has been used for keratinocyte isolation and staining.[1] 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.[2]

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

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

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.

Disclaimer

This product should be stored frozen at -20°C

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

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

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T5266

Trypsin from porcine pancreas

technique(s)

cell culture | mammalian: suitable

technique(s)

-

technique(s)

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

technique(s)

cell culture | mammalian: suitable

biological source

Porcine pancreas

biological source

-

biological source

Porcine pancreas

biological source

Porcine pancreas

concentration

1 ×

concentration

-

concentration

25 mg/mL

concentration

25 mg/mL

form

solution

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

mol wt

23.4 kDa

mol wt

23.8 kDa

mol wt

23.8 kDa

mol wt

23.8 kDa

shipped in

dry ice

shipped in

-

shipped in

ambient

shipped in

wet ice

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Storage Class

12 - Non Combustible Liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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