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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
Synonim(y):
Cocoonase, Tryptar, Tryptase
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About This Item
Polecane produkty
pochodzenie biologiczne
Porcine
Poziom jakości
sterylność
sterile-filtered
linia produktu
BioReagent
Formularz
solution
masa cząsteczkowa
23.4 kDa
stężenie
10 ×
metody
cell culture | mammalian: suitable
zanieczyszczenia
Porcine parvovirus, none detected (9 CFR)
pH
7.0-7.6
Warunki transportu
dry ice
temp. przechowywania
−20°C
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Zastosowanie
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
Działania biochem./fizjol.
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.
Komponenty
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.
Przestroga
This product is stored frozen between -10 and -40°C. Repeated cycles of freezing and thawing should be avoided.
Uwaga dotycząca przygotowania
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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Numer produktu
Opis
Cennik
polecane
Kod klasy składowania
12 - Non Combustible Liquids
Klasa zagrożenia wodnego (WGK)
WGK 1
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
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Protokoły
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.
Trypsyna jest powszechnie stosowana do oddzielania przylegających komórek od powierzchni. Dostępna jest szeroka gama roztworów trypsyny, aby spełnić specyficzne wymagania linii komórkowej.
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