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)
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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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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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
Kelly Huber et al.
Molecular cancer therapeutics, 7(1), 143-151 (2008-01-19)
2-[(1-methylpropyl)dithio]-1H-imidazole (IV-2) is a known inhibitor of the thioredoxin system. It causes the oxidation of cysteine residues from both thioredoxin reductase and thioredoxin, with only the latter leading to irreversible inhibition of protein function. Although IV-2 is considered to be
E Saitoh et al.
Archives of biochemistry and biophysics, 352(2), 199-206 (1998-05-20)
Two variants of cystatin SA encoded by two alleles at the CST2 locus of the type 2 human cystatin gene family were expressed in Escherichia coli. One, termed cystatin SA1, is identical to cystatin SA [S. Isemura, E. Saitoh, and
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