All Photos(1)



Trypsin-EDTA solution

10 ×, sterile-filtered, BioReagent, suitable for cell culture, 5.0 g porcine trypsin and 2 g EDTA • 4Na per liter of 0.9% sodium chloride

Cocoonase, Tryptase, Tryptar
Enzyme Commission number:
MDL number:

biological source


Quality Level



product line




mol wt

23.4 kDa


10 ×


cell culture | mammalian: suitable


Porcine parvovirus, none detected (9 CFR)



shipped in

dry ice

storage temp.


Looking for similar products? Visit Product Comparison Guide


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 is used for the following applications:
  • Used as a supplement in cell culture for their maintenance
  • In harvesting cells grown to confluence
  • to detach lentivirus-transduced macrophages

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.


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.


This product is stored frozen between -10 and -40°C. Repeated cycles of freezing and thawing should be avoided.

Preparation Note

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 contaiing no Ca2+ or Mg2+.

Storage Class Code

12 - Non Combustible Liquids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Origin

Enter Lot Number to search for Certificate of Origin (COO).

George R Wendt et al.
eLife, 7 (2018-03-21)
Schistosomes infect more than 200 million people. These parasitic flatworms rely on a syncytial outer coat called the tegument to survive within the vasculature of their host. Although the tegument is pivotal for their survival, little is known about maintenance
Nadja S Katheder et al.
Nature, 541(7637), 417-420 (2017-01-13)
As malignant tumours develop, they interact intimately with their microenvironment and can activate autophagy, a catabolic process which provides nutrients during starvation. How tumours regulate autophagy in vivo and whether autophagy affects tumour growth is controversial. Here we demonstrate, using
Xinyun Huang et al.
Acta biochimica et biophysica Sinica, 50(9), 853-861 (2018-07-31)
Cholesterol is one of the major components of biological membranes and has an important function in osteoclast formation and survival. It has been reported that high-density lipoprotein (HDL) promotes cholesterol efflux from osteoclasts and induces their apoptosis, but the underlying
Guosong Qiu et al.
Journal of lipid research, 48(2), 385-394 (2006-11-10)
LPL and endothelial lipase (EL) are associated with macrophages in human atherosclerotic lesions, and overexpression of LPL in mouse macrophages is associated with a greater extent of atherosclerosis. To investigate potential mechanisms by which macrophage-derived lipase expression may mediate proatherogenic
Denisa Beňová-Liszeková et al.
Microscopy research and technique, 82(7), 1145-1156 (2019-03-27)
Although scanning electron microscopy (SEM) has been broadly used for the examination of fixed whole insects or their hard exoskeleton-derived structures, including model organisms such as Drosophila, the routine use of SEM to evaluate vulnerable soft internal organs and tissues


Cell Dissociation Protocol with Trypsin

Trypsin is frequently used in cell dissociation from adherent surfaces. We offer a wide variety of trypsin solutions to meet your specific cell line requirements, as well as protocols, troubleshooting ideas, and more.

Related Content

Trypsin Serine Protease Enzyme

Trypsin is an enzyme in the serine protease class that consists of a polypeptide chain of 223 amino acid residues. Multiple sources, grades and formulations of trypsin specifically designed for research applications are available.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service