F4165
Ficin from fig tree latex
powder, ≥0.1 unit/mg solid
Synonym(s):
Debricin, Ficain, higueroxyl delabarre
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About This Item
Recommended Products
biological source
fig tree (latex)
Quality Level
form
powder
specific activity
≥0.1 unit/mg solid
mol wt
23.8 kDa
storage temp.
−20°C
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General description
Extinction Coefficient: E1% = 21.0 (280 nm)
pI: 9.0
pI: 9.0
Biochem/physiol Actions
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-nitroanilide is 0.43 mM. Ficin is inhibited by iodoacetamide, iodoacetic acid, N-ethylmaleimide, mercuric chloride, DFP (diisopropyl fluorophosphate), TLCK (Na-p-Tosyl-lysine chloromethyl ketone), and TPCK (N-Tosyl-L-phenylalanine chloromethyl ketone). Ficin can be used to generate high yielding F (ab′)2 fragments from mouse IgG1.
Unit Definition
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.
inhibitor
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Description
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substrate
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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)
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Customers Also Viewed
Yufang Yang et al.
Scientific reports, 7, 43141-43141 (2017-02-23)
Ficin is classified as a sulfhydryl protease isolated from the latex of fig trees. In most cases, a particular enzyme fits a few types of substrate and catalyzes one type of reaction. In this investigation, we found sufficient proofs for
H Sekizaki et al.
Amino acids, 34(1), 149-153 (2007-07-10)
The capability of ficin, a cystine protease, to form peptide bonds was investigated using several types of N-Boc-amino acid phenyl and naphthyl esters as acyl donor components. Enzyme-catalyzed peptide synthesis was carried out under optimized reaction conditions of pH, acyl
Kristien Bonroy et al.
Journal of immunological methods, 312(1-2), 167-181 (2006-05-06)
The sensitivity of immunosensors is strongly dependent on the amount of immobilised antibodies and their remaining antigen binding properties. The use of smaller and well-oriented antibody fragments as bioreceptor molecules influences the final immunosensor signal. The aim of this study
Eiichi Saitoh et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 141(1), 103-109 (2005-04-12)
A novel cysteine protease inhibitor (Eel-CPI-1) was isolated from the epidermis of the eel. Eel-CPI-1 was shown to bind strongly to both lactose- and carboxymethylated papain-affinity gels. Its molecular mass under reducing condition was determined to be 18 kDa by
Miriam Fogg Leach et al.
Transfusion, 42(4), 476-480 (2002-06-22)
Solid-phase RBC adherence (SPRCA) assays (Immucor) detect HLA and/or platelet-specific antibodies. Pretreatment of reagent platelets with enzymes was investigated to determine whether the sensitivity of the assay could be increased. SPRCA testing, following the manufacturer's directions, was performed on 51
Protocols
This procedure may be used for all Ficin products.
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