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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

Synonym(s):

Cocoonase, Tryptar, Tryptase

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About This Item

MDL number:
MFCD00130286
UNSPSC Code:
12352204
NACRES:
NA.75

biological source

Porcine pancreas

Quality Level

300

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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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

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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Carlos Pantoja et al.
Current biology : CB, 30(18), 3647-3656 (2020-08-09)
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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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