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F4165

Sigma-Aldrich

Ficin from fig tree latex

powder, ≥0.1 unit/mg solid

Synonym(s):

Debricin, Ficain, higueroxyl delabarre

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About This Item

CAS Number:
9001-33-6
Enzyme Commission number:
3.4.22.3 (BRENDA, IUBMB)
EC Number:
232-599-1
MDL number:
MFCD00081597
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

fig tree (latex)

Quality Level

200

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

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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Description
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pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Pepsin lyophilized (salt-free), ~2500 units/mg protein (At 37 °C with hemoglobin as the substrate. One unit is the enzyme activity which liberates the amount of Tyr producing an increase in the absorbance of 0.001/minute at 280 nm.)

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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
Kamsagara Basavarajappa Devaraj et al.
Journal of agricultural and food chemistry, 56(23), 11417-11423 (2008-11-11)
Ficin (EC 3.4.22.3), a cysteine proteinase isolated from the latex of a Ficus tree, is known to occur in multiple forms. Although crude ficin is of considerable commercial importance, ficin as such has not been fully characterized. A major ficin
Andrey V Sorokin et al.
Polymers, 14(11) (2022-06-11)
This work aims to synthesize graft copolymers of chitosan and N-vinylimidazole (VI) with different compositions to be used as matrices for the immobilization of cysteine proteases-bromelain, ficin, and papain. The copolymers are synthesized by free radical solution copolymerization with a
Daniel Janvier et al.
Transfusion, 53(9), 1948-1955 (2012-12-18)
Rh proteins and the Wr(b) antigen, which results from an interaction between Band 3 and glycophorin A, are the most common targets for warm immunoglobulin (Ig)G autoantibodies. Apart from autoanti-Di(b) , a scarce specificity, IgG warm autoantibodies specific for Band
S Fadýloğlu
Die Nahrung, 45(2), 143-146 (2001-05-31)
Fig tree latex (ficin) was immobilized on Celite by adsorption. The free and immobilized ficin were utilized in the production of teleme (a Turkish milk product). After immobilization, the optimal temperature of ficin was shifted from 60 to 80 degrees
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Protocols

Enzymatic Assay of Ficin (EC 3.4.22.3)

This procedure may be used for all Ficin products.

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