Trypsin 1-250, virus free

Key Features and Details

Trypsin 1-250, Virus Free

SYNONYMS: Parenzymol; Parenzyme; Tryptar; Trypure; U-4858
CAS: # 9002-07-7
EC No: 232-650-8
MDL No: MFCD00082094

You need to register an account with us
to be able to place an order, Click to Register.

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
Base Catalog Number: 153571
Alternate Names: Parenzymol; Parenzyme; Tryptar; Trypure; U-4858
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 No : 232-650-8
Extinction Coefficient : 14.3
Format : White powder
Grade : ?-irradiated, Virus Free
Isoelectric Point : 10.5
MDL No : MFCD00082094
Protein or Enzyme Type : Proteins, Enzymes & Peptides
RTECS No : 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 : ?-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.

© All rights reserved byJuniperlifesciences.com 2021

All logos and Trademarks are names the property of their respective owners.

Shopping Cart
Scroll to Top

Enquire

Submit your details and receive all the download links in your email

Login to your account
Login to your account