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Merck

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

Synonim(y):

Cocoonase, Tryptar, Tryptase

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About This Item

Numer MDL:
Kod UNSPSC:
12352204
NACRES:
NA.75

pochodzenie biologiczne

Porcine pancreas

sterylność

sterile-filtered

linia produktu

BioReagent

Postać

solution

stężenie

1 ×

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. It can be used with endothelial cell cultures.

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.

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.
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Kod klasy składowania

12 - Non Combustible Liquids

Klasa zagrożenia wodnego (WGK)

nwg

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

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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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