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T4299

Sigma-Aldrich

Trypsin-EDTA solution

1 ×, sterile-filtered, BioReagent, suitable for cell culture, 500 BAEE units porcine trypsin and 180 μg EDTA, 4Na per ml in Dulbecco′s PBS without calcium and magnesium

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

biological source

Porcine pancreas

sterility

sterile-filtered

product line

BioReagent

form

solution

concentration

1 ×

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
T4174T4049T3449
Sigma-Aldrich

Sigma-Aldrich

T4299

Trypsin-EDTA solution

Sigma-Aldrich

Sigma-Aldrich

T4174

Trypsin-EDTA solution

Sigma-Aldrich

Sigma-Aldrich

T4049

Trypsin-EDTA solution

sterility

sterile-filtered

sterility

sterile-filtered

sterility

sterile-filtered

sterility

sterile-filtered

form

solution

form

solution

form

solution

form

aqueous solution

concentration

1 ×

concentration

10 ×

concentration

0.25%

concentration

1 ×

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

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

technique(s)

cell culture | mammalian: suitable

impurities

Porcine parvovirus, none detected (9 CFR)

impurities

Porcine parvovirus, none detected (9 CFR)

impurities

Porcine parvovirus, none detected (9 CFR)

impurities

-

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. It can be used with endothelial cell cultures.

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.

Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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25G
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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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