Merck
All Photos(1)

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, Tryptase, Tryptar
Número MDL:
NACRES:
NA.75

origen biológico

Porcine pancreas

Nivel de calidad

400

esterilidad

sterile-filtered

línea de producto

BioReagent

formulario

solution

concentración

1 ×

technique(s)

cell culture | mammalian: suitable

impurezas

Porcine parvovirus, none detected (9 CFR)

pH

7.0-7.6

enviado en

dry ice

temp. de almacenamiento

−20°C

Looking for similar products? Visit Product Comparison Guide

Related Categories

Aplicación

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.

Acciones bioquímicas o fisiológicas

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.

Componentes

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.

Precaución

This product is stored frozen between -10 and -40°C. Repeated cycles of freezing and thawing should be avoided.

Código de clase de almacenamiento

12 - Non Combustible Liquids

WGK

nwg

Punto de inflamabilidad F

Not applicable

Punto de inflamabilidad C

Not applicable

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Origin

Enter Lot Number to search for Certificate of Origin (COO).

Protocols

Cell Dissociation Protocol using Trypsin

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.

Related Content

Trypsin Serine Protease Enzyme

Trypsin is an enzyme in the serine protease class that consists of a polypeptide chain of 223 amino acid residues. Multiple sources, grades and formulations of trypsin specifically designed for research applications are available.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service