T7409
Trypsin from porcine pancreas
lyophilized powder, Type II-S, 1,000-2,000 units/mg dry solid
Sign Into View Organizational & Contract Pricing
All Photos(3)
About This Item
Recommended Products
type
Type II-S
form
lyophilized powder
specific activity
1,000-2,000 units/mg dry solid
mol wt
23.8 kDa
storage temp.
−20°C
Looking for similar products? Visit Product Comparison Guide
Related Categories
Application
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 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.
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.
Components
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.
Caution
Solutions in 1 mM HCl are stable for 1 year in aliquots and stored at -20°C. The presence of Ca2+ will also diminish the self-autolysis of trypsin and maintain its stability in solution. Trypsin will also retain most of its activity in 2.0 M urea, 2.0 M guanidine HCl, or 0.1% (w/v) SDS.
Unit Definition
One BAEE unit will produce a ΔA253 of 0.001 per min at pH 7.6 at 25° C using BAEE as substrate. One BTEE unit = 320 ATEE units. Reaction volume = 3.2 mL (1 cm light path).
Preparation Note
This product is a lyophilized powder soluble in Hank′s Balanced Salt Solution at 25 mg/mL.
inhibitor
Product No.
Description
Pricing
substrate
Product No.
Description
Pricing
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
Tanja Laske et al.
PLoS computational biology, 15(4), e1006944-e1006944 (2019-04-12)
The best measure to limit spread of contagious diseases caused by influenza A viruses (IAVs) is annual vaccination. The growing global demand for low-cost vaccines requires the establishment of high-yield production processes. One possible option to address this challenge is
Daniel Rüdiger et al.
PLoS computational biology, 15(2), e1006819-e1006819 (2019-02-20)
Influenza A viruses (IAV) are commonly used to infect animal cell cultures for research purposes and vaccine production. Their replication is influenced strongly by the multiplicity of infection (MOI), which ranges over several orders of magnitude depending on the respective
Elgin Turkoz Uluer et al.
American journal of translational research, 13(6), 6236-6247 (2021-07-27)
The aim of this study was to show the effects of autophagy inhibitor Wortmannin and antiangiogenic-proapoptotic Thalidomide on autophagy and apoptosis markers in 4T1 breast cancer cells in vitro and in vivo. The half-maximal inhibitory concentration (IC50) values of 4T1
Xiaoyu Zou et al.
Frontiers in nutrition, 7, 151-151 (2020-10-20)
In this work, we investigated changes in protein structures in vacuum-packed pork during chill storage and its impact on the in vitro protein digestion. Longissimus dorsi muscles were vacuum packed and stored at 4°C for 3 days. Samples were subjected
Andreia Vasconcelos et al.
Biomacromolecules, 9(4), 1299-1305 (2008-03-22)
Wool and silk were dissolved and used for the preparation of blended films. Two systems are proposed: (1) blend films of silk fibroin and keratin aqueous solutions and (2) silk fibroin and keratin dissolved in formic acid. The FTIR spectra
Protocols
Continuous spectrophotometric rate determination method using BAEE substrate measures trypsin activity, essential for enzyme characterization.
Use this protocol to for the entire immunohistochemistry (IHC) procedure through staining and visualization of specific antigens in paraffin-embedded tissue sections.
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