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.
ApplicationThe 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
Features and BenefitsStableCell™ trypsin is formulated as a gentle solution for cell detachment. Enzyme activity is retained when stored at 2-8°C, and our studies even show >90% activity is retained when left at room temperatures for up to 7 weeks!
- Save Time - no more freeze or thaw cycles
- Save Space - store at 2-8°C and free up your freezer
- Does not need to be aliquoted
- Only the best for your cells - manufactured in GMP environment