T4299
Solution de trypsine-EDTA
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
Synonyme(s) :
Cocoonase, Tryptar, Tryptase
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| Conditionnement | Référence | Disponibilité | Prix |
|---|
A propos de cet article
Biological source:
Porcine pancreas
Concentration:
1 ×
Le tarif et la disponibilité ne sont pas disponibles actuellement.
Service technique
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Laissez-nous vous aiderbiological source
Porcine pancreas
Quality Level
sterility
sterile-filtered
product line
BioReagent
form
solution
concentration
1 ×
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
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. It can be used with endothelial cell cultures.
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.
Other Notes
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.
Disclaimer
This product is stored frozen between -10 and -40°C. Repeated cycles of freezing and thawing should be avoided.
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Cet article | |||
|---|---|---|---|
| technique(s) cell culture | mammalian: suitable | technique(s) cell culture | mammalian: suitable | technique(s) cell culture | mammalian: suitable, single cell analysis: suitable | technique(s) cell culture | mammalian: suitable, single cell analysis: suitable |
| biological source Porcine pancreas | biological source Porcine | biological source Porcine | biological source Porcine |
| concentration 1 × | concentration 10 × | concentration 0.25% | concentration 1 × |
| form solution | form solution | form solution | form solution |
| shipped in dry ice | shipped in dry ice | shipped in dry ice | shipped in dry ice |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
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Classe de stockage
12 - Non Combustible Liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
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Numéro d'article de commerce international
| Référence | GTIN |
|---|---|
| T4299-100ML | 04061837345708 |