Sigma-Aldrich T3924 Trypsin-EDTA solution 100 mL
Marka
Stok Kodu
LB.SA.T3924-100ML
Kısa Bilgi
1 ×, sterile; sterile-filtered, BioReagent, suitable for cell culture, 0.5 g porcine trypsin and 0.2 g EDTA, 4Na per liter of Hanks′ Balanced Salt Solution with phenol red
| Sigma-Aldrich T3924 Trypsin-EDTA solution 100 mL |
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Synonym(s): Cell dissociation enzyme
Enzyme Commission number: 3.4.21.4 (BRENDA, IUBMB)
MDL number: MFCD00130286
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PROPERTIES
biological source Porcine
Quality Level 400
sterility sterile; 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 7.0-9.0
shipped in dry ice
storage temp. −20°C
DESCRIPTION
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.
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.
Components
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.
Caution
This product is stored frozen between -10 and -40°C. Repeated cycles of freezing and thawing should be avoided.
Preparation Note
This product does contain phenol red. Due to shipment on dry ice, there could be significant carbon dioxide buildup in the package. This CO2 may enter the solution and lower the pH slightly, giving an orange rather than pinkish color. The orange solution will still be suitable for use, or the pH can be adjusted with sodium hydroxide. 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 containing no Ca2+ or Mg2+. |
