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.
| Trypsin EDTA solution 0.25%, sterile-filtered, BioReagent, suitable for cell culture, 2.5 g porcine trypsin and 0.2 g EDTA, 4Na per liter of Hanks′ Balanced Salt Solution with phenol red - Details | |
| source | Porcine |
| sterility | sterile-filtered |
| mol wt | 23.4 kDa |
| concentration | 0.25% |
| technique | cell culture | mammalian: suitable | single cell analysis: suitable |
| impurities | Porcine parvovirus, none detected (9 CFR) |
| pH | 7.0-7.6 |
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 was used:
- in detaching HT29 human colorectal cancer cells cultured in RPMI 1640 which was supplemented with 10 % fetal calf serum, during relative cell frequency determination of high concentration samples
- to trypsinize the transient transfected human embryonic kidney tcA-201 cell line.
- to enzymatically release mouse fibroblasts cells (cell line L929) adhered to the scaffold, during cell culturing to assess the influence of several modified treatments of Poly(L/D)lactide 96/4 non-woven scaffolds and fibres
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