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T4174

Sigma-Aldrich

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

Synonym(s):

Cocoonase, Tryptar, Tryptase

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About This Item

Enzyme Commission number:
3.4.21.4 (BRENDA, IUBMB)
MDL number:
MFCD00130286
UNSPSC Code:
12352204
NACRES:
NA.75

biological source

Porcine

Quality Level

400

sterility

sterile-filtered

product line

BioReagent

form

solution

mol wt

23.4 kDa

concentration

10 ×

technique(s)

cell culture | mammalian: suitable

impurities

Porcine parvovirus, none detected (9 CFR)

pH

7.0-7.6

shipped in

dry ice

storage temp.

−20°C

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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 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.

Components

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.

Caution

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+.

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Protocols

Trypsin Cell Dissociation Protocol

Trypsin is commonly used for dissociating adherent cells from surfaces. A wide variety of trypsin solutions are available to meet your specific cell line requirements.

Trypsin Cell Dissociation Protocol

Trypsin is commonly used for dissociating adherent cells from surfaces. A wide variety of trypsin solutions are available to meet your specific cell line requirements.

Trypsin Cell Dissociation Protocol

Trypsin is commonly used for dissociating adherent cells from surfaces. A wide variety of trypsin solutions are available to meet your specific cell line requirements.

Trypsin Cell Dissociation Protocol

Trypsin is commonly used for dissociating adherent cells from surfaces. A wide variety of trypsin solutions are available to meet your specific cell line requirements.

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