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.
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Trypsin-EDTA solution
Details
Category:
detachment enzyme
Manufacture:
Sigma Aldrich
| sterility | sterile; sterile-filtered |
| product line | BioReagent |
| concentration | 1 × |
| application(s) | cell culture | mammalian: suitable |
| impurities | Porcine parvovirus, none detected (9 CFR) |
| pH-range | 7.0 – 7.6 |
| storage temp. | −20°C |
| T3924 | Trypsin-EDTA solution 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 |
| T3449 | TrypZean® Solution, 1× recombinant, expressed in corn, sterile-filtered |
Brochure
CoA
SDS
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.