T8802
Trypsin from bovine pancreas
TPCK Treated, essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein
About This Item
Recommended Products
biological source
bovine pancreas
Quality Level
sterility
aseptically filled
form
essentially salt-free, lyophilized powder
specific activity
≥10,000 BAEE units/mg protein
mol wt
23.8 kDa
composition
protein, ≥95%
solubility
hydrochloric acid: soluble 1 mM, clear
foreign activity
Chymotrypsin ≤0.1 BTEE units/mg protein
storage temp.
−20°C
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General description
Application
Biochem/physiol Actions
Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin.
Unit Definition
Preparation Note
Analysis Note
Other Notes
Substrate
inhibitor
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Protocols
This procedure is for products with a specification for Trypsin activity using Na-Benzoyl-L-arginine ethyl ester (BAEE) as a substrate. The procedure is a continuous spectrophotometric rate determination (A253, Light path = 1 cm).
Related Content
Trypsin is an enzyme in the serine protease class that consists of a polypeptide chain of 223 amino acid residues. Multiple sources, grades and formulations of trypsin specifically designed for research applications are available.
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
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