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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

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Synonym(s):
Cocoonase, Tryptar, Tryptase
Enzyme Commission number:
MDL number:
NACRES:
NA.75

biological source

Porcine

Quality Level

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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This Item
T404912736C12731C
Sigma-Aldrich

Sigma-Aldrich

T4174

Trypsin-EDTA solution

Sigma-Aldrich

Sigma-Aldrich

T4049

Trypsin-EDTA solution

Sigma-Aldrich

Sigma-Aldrich

12736C

Porcine Serum

Sigma-Aldrich

Sigma-Aldrich

12731C

Porcine Serum

sterility

sterile-filtered

sterility

sterile-filtered

sterility

sterile-filtered

sterility

sterile-filtered

form

solution

form

solution

form

-

form

-

mol wt

23.4 kDa

mol wt

23.4 kDa

mol wt

-

mol wt

-

concentration

10 ×

concentration

0.25%

concentration

-

concentration

-

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable, single cell analysis: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

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+.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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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

Protocols

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.

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

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