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Key Documents

T2601

Sigma-Aldrich

Solution de trypsine-EDTA

1X, sterile-filtered, BioReagent, suitable for cell culture, 0.5 g porcine trypsin and 0.2 g EDTA, 4Na per liter of Hanks′ Balanced Salt Solution with phenol red

Synonyme(s) :

Trypsin-EDTA solution

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About This Item

Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.78

Niveau de qualité

Stérilité

sterile-filtered

Gamme de produits

BioReagent

Concentration

1X

Technique(s)

cell culture | mammalian: suitable

Conditions d'expédition

wet ice

Température de stockage

2-8°C

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Description générale

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.

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.

Actions biochimiques/physiologiques

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. Ethylenediaminetetraacetic acid (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.

Caractéristiques et avantages

StableCell trypsin is formulated as a gentle solution for cell detachment. Enzyme activity is retained when stored at 2-8°C, and our studies even show >90% activity is retained when left at room temperatures for up to 7 weeks!
  • Save Time - no more freeze or thaw cycles
  • Save Space - store at 2-8°C and free up your freezer
  • Does not need to be aliquoted
  • Only the best for your cells - manufactured in GMP environment

Notes préparatoires

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 containing no Ca2+ or Mg2+.

Stockage et stabilité

Recommended storage is 2-8°C upon arrival. During stability studies, data showed that this product retains ≥90% of its activity when stored at 37°C for up to 8 weeks.

Informations légales

StableCell is a trademark of Sigma-Aldrich Co. LLC

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Methods of Enzymatic Analysis (1965)
Multiplexed isobaric tagging protocols for quantitative mass spectrometry approaches to auditory research.
Vetter D E, et al.
Methods in Molecular Biology, 493, 345-366 (2009)
Ryan Calcutt et al.
Science advances, 7(43), eabj1469-eabj1469 (2021-10-21)
[Figure: see text].

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Protocoles

StableCell™ Trypsin solutions are designed to perform cell detachment as standard trypsin solutions do, without the need to aliquot, freeze, and thaw. This saves significant time before passaging.

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