E.coli Recombinant Trypsin Animal Origin Free Trypsin 3800 USP u/mg
Trypsin is a member of the serine protease family. Trypsin cleaves
peptides on the C-terminal end of lysine and arginine amino acid
residues. The optimum pH of trypsin is pH 7 - 10. The enzyme is
inhibited by serine protease inhibitors, e.g. PMSF and by metal
The activity of most Sigma preparations is determined by a
continuous rate spectrophotometric assay
and expressed in BAEE units.
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.
Reaction volume = 3.2 mL (1 cm light path).
Temp = 25 °C, pH = 7.6, A253nm, Light path = 1 cm
In a 3.2 ml reaction mix, the final concentrations are 63 mM sodium
phosphate, 0.23 mM Nα-benzoyl-L-arginine ethyl ester, 0.06 mM
hydrochloric acid, and 100 units trypsin.
1 BAEE µM Unit = 200 BAEE Units
1 TAME µM Unit = 0.27 BAEE µM Units
1 BAEE µM Unit = 3.64 TAME Units
1 TAME µM Unit = 55 BAEE A253 Units
1 BAEE A253 Unit = 0.018 TAME µM Unit
1 TAME µM Unit = 180 TAME A247 Units
1 TAME A247 Unit = 0.33 BAEE Units
1 USP Unit = 3.0 BAEE Units
1 NF Unit = 1.1 USP Units
Recombinant Porcine Trypsin is a genetically engineered protein
expressed in E.coli and purified
by high pressure liquid chromatography. There are no contaminating
enzyme activities such as carboxypeptidase A and chymotrypsin. No
protease inhibitors such as PMSF are contained in the preparation.
Animal origin free:The use of recombinant Porcine Trypsin eliminates the risk of virus
and other potential adventitious agents found in animal-derived
YaxinBio Recombinant Porcine Trypsin belongs to the AOF level 3.
Stablility:A sterile recombinant trypsin lyophilized powder eliminates the
contamination risks and decreases the chance of activity loss in
the process of transport and storage.
1) Recombinant porcine trypsin provides increased specific activity
and eliminates contaminating proteases activities found in
2) No other contaminating proteases such as chymotrypsin or
NLT 70% β-trysin, NMT 20% α-trypsin
No chymotrypsin, carboxypeptidase A, and other protease
Prepare 1-10mg/ml recombinant trypsin with 1mM HCl.The ratio to
aimed protein is 1:50
to 1:1000 (w/w).The optimum pH is pH7-10.
Recombinant trypsin lyophilized should be stored under 2℃-8℃ in
sealed container. It is
stable within 24 months.After dissolved, it should be stored under
-20℃. It is stable within
24 months and above 90% activity remained after 10 times repeated
freezing and thawing.