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T4174
Trypsin-EDTA solution
10 ×, sterile-filtered, BioReagent, suitable for cell culture, 5.0 g porcine trypsin and 2 g EDTA, 4Na per liter of 0.9% sodium chloride
Trypsin-EDTA solution
Synonym(s):
Cocoonase, Tryptar, Tryptase
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About This Item
Biological source:
Porcine
Concentration:
10 ×
Pricing and availability is not currently available.
biological source
Porcine
Quality Level
sterility
sterile-filtered
product line
BioReagent
form
solution
mol wt
23.4 kDa
concentration
10 ×
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
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.
Trypsin-EDTA solution is used for the following applications:
Trypsin-EDTA solution is used for the following applications:
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.
Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin.
Preparation Note
Incubating cells with too high a trypsin concentration for a long period can damage cell membranes and kill the cells. Solubilizing trypsin or diluting it from a concentrated solution should be done with a buffered salt solution contaiing no Ca2+ or Mg2+.
Other Notes
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
This product is stored frozen between -10 and -40°C. Repeated cycles of freezing and thawing should be avoided.
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This Item | |||
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| technique(s) cell culture | mammalian: suitable | technique(s) cell culture | mammalian: suitable | technique(s) cell culture | mammalian: suitable, single cell analysis: suitable | technique(s) cell culture | mammalian: suitable, single cell analysis: suitable |
| biological source Porcine | biological source Porcine pancreas | biological source Porcine | biological source Porcine |
| form solution | form solution | form solution | form solution |
| concentration 10 × | concentration 1 × | concentration 0.25% | concentration 1 × |
| shipped in dry ice | shipped in dry ice | shipped in dry ice | shipped in dry ice |
| mol wt 23.4 kDa | mol wt - | mol wt 23.4 kDa | mol wt 23.4 kDa |
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Storage Class
12 - Non Combustible Liquids
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.
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Global Trade Item Number
| SKU | GTIN |
|---|---|
| T4174-20ML | 04061838260093 |
| T4174-500ML | 04065273466058 |
| T4174-100ML | 04061838260086 |