T4424

Trypsin solution from porcine pancreas

1 ×, sterile-filtered, BioReagent, suitable for cell culture, 2.5 g porcine trypsin per liter in Hanks′ Balanced Salt Solution with phenol red

• Número CAS: 9002-07-7
• Número da licença da enzima: 3.4.21.4 (BRENDA, IUBMB)
• Número MDL: MFCD00082094
• Código UNSPSC: 12352204
• NACRES: NA.75

Propriedades

• fonte biológica: Porcine pancreas
• Nível de qualidade: 400
• esterilidade: sterile-filtered
• linha de produto: BioReagent
• Formulário: solution
• peso molecular: 23.4 kDa
• concentração: 1 ×
• técnica(s): cell culture | mammalian: suitable
• Impurezas: Porcine parvovirus, none detected (9 CFR)
• pH: 7.0-7.6
• Condições de expedição: dry ice
• temperatura de armazenamento: −20°C

Descrição

Aplicação

Trypsin solution from porcine pancreas has been used for keratinocyte isolation and staining.[1] It has also been used as a component of CMF-Steinberg′s solution to replace heart tissues after centrifugation in a study to culture embryonic cardiomyocytes from Mexican axolotl.[2]

For trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide. 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. Trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestions. Additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps.

Ações bioquímicas/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.

Atenção

This product should be stored frozen at -20°C

Definição da unidade

One BAEE unit will produce a A₂₅₃ of 0.001 per minute at pH 7.6 at 25°C using BAEE as a substrate.

Nota de preparo

This is a 2.5 g/L porcine trypsin solution in Hank′s Balanced Salt Solution with phenol red.

Informações de segurança

• Código de classe de armazenamento: 12 - Non Combustible Liquids
• Classe de risco de água (WGK): WGK 3
• Ponto de fulgor (°F): Not applicable
• Ponto de fulgor (°C): Not applicable