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Trypsin 1-250, virus free

Trypsin 1-250, virus free

$310.00

Trypsin 1-250, Virus Free

SKU: 02153571-CF

Synonyms
Parenzymol; Parenzyme; Tryptar; Trypure; U-4858
CAS Number:
9002-07-7
EC Number:
232-650-8
MDL Number:
MFCD00082094
Product Description

Trypsin 1-250, Virus Free

Application Notes

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 digestionsns†. 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.Trypsin Powder, Porcine 1:250 is used to release adherent cells from tissue culture plates for passaging. It was used in the isolation and culture of human endothelial cells.

Usage Statement

Unless specified otherwise, MP Biomedical's products are for research or further manufacturing use only, not for direct human use. For more information, please contact our customer service department.

Specifications
SKU 02153571-CF
Alternate Names Parenzymol; Parenzyme; Tryptar; Trypure; U-4858
Application Notes 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 digestionsns†. 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.Trypsin Powder, Porcine 1:250 is used to release adherent cells from tissue culture plates for passaging. It was used in the isolation and culture of human endothelial cells.
Base Catalog Number 153571
Biochemical Physiological 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.
CAS # 9002-07-7
EC Number 232-650-8
Extinction Coefficient 14.3
Format White powder
Grade γ-irradiated, Virus Free
Isoelectric Point 10.5
Protein or Enzyme Type Proteins, Enzymes & Peptides
RTECS Number YN5075000
Source Porcine
Specific Activity >250 U/mg
Specificity The protease activity of trypsin is highly specific toward positively charged side chains with lysine and arginine. Forms complexes with a2-macroglobulin. Can be used in the isolation of intact; detergent-free phycobilisomes and in the hydrolysis/condensation of carboxylic ester bonds.
Sterility γ-Irradiated
Typical Working Concentration For trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide.
Unit Definition The activity causing a change in absorbance of 0.003/minute at 253 nm.
Usage Statement Unless specified otherwise, MP Biomedical's products are for research or further manufacturing use only, not for direct human use. For more information, please contact our customer service department.
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