T4174
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
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.75
Recommended Products
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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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:
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.
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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also commonly purchased with this product
Product No.
Description
Pricing
recommended
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 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.
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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