Trypsin is a proteolytic enzyme used to detach adherent cell from culture vessel surfaces. Typical use includes 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 is a serine protease derived from porcine pancreas. It is a single chain polypeptide of 223 amino acid residue with substrate specificity based on positively charged Lysine and Arginine side chains. Trypsin predominantly cleaves peptide chains at the carboxyl sides of Lysine and Arginine, except when either is followed by Proline. It is most commonly used for dissociation and disaggregation of adherent cells.
Ethylenediaminetetraacetic acid (EDTA), a chelating agent often added to enhance enzymatic activity of trypsin solution. EDTA acts by neutralizing calcium and magnesium ions that enhance cell-to-cell adhesion.
Trypsin, 0.05% – EDTA, 0.1% assists in the dissociation of cell monolayers and tissue; most useful when dissociating fibroblasts and keratinocytes. While, Trypsin, 0.25% – EDTA, 0.02%, assists in detaching normal and transformed cells from vessel surfaces.
Max Shelf Life: 24 months
Storage Conditions: -10°C to -20°C
Shipping Condition: on dry ice*
Harmonization Code: 3822.00.5090
*NOTE: During shipping, the trypsin might change color from pink to yellow due to exposure to carbon dioxide released from the dry ice in the shipping container. In our experience, this discoloration does not effect the functionality of the trypsin.