|Related Categories||3.4.x.x Peptidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Enzyme Class Index,|
|mol wt||mol wt 23.8 kDa|
Extinction Coefficient: E1% = 21.0 (280 nm)
One unit will produce a ΔA280 of 1.0 per min at pH 7.0 at 37 °C when measuring TCA soluble products from casein in a final volume of 10 ml (1 cm light path).
The enzyme is soluble in 1 M potassium phosphate buffer, pH 7.0 (0.25 mg/ml), yielding a clear solution.
Ficin is classified as a thiol protease. It contains a single reactive cysteine at its active site. The amino acid homology of the active site is similar to that of papain. Ficin will cleave proteins at the carboxyl side of Gly, Ser, Thr, Met, Lys, Arg, Tyr, Ala, Asn, and Val. The reported Km for the chromogenic substrate pGlu-Phe-Leu-p-nitroanili
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|Precautionary statements||P261-P305 + P351 + P338-P342 + P311|
|Personal Protective Equipment||dust mask type N95 (US), Eyeshields, Faceshields, Gloves|
|Hazard Codes (Europe)||Xn|
|Risk Statements (Europe)||36/37/38-42|
|Safety Statements (Europe)||22-24-26-36/37|
1. OBJECTIVE To standardize a procedure for determining the activity of Ficin by enzymatic analysis.
Glazer, A. N., and Smith, E. L. The Enzymes 3rdth ed., New York, NY , (1971), 538-542
Ficin Liener, I. E., and Friedenson, B. Meth. Enzymol. 19, 261-273, (1970)
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