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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:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

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

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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Pictograms

Health hazardExclamation mark

Signal Word

Danger

Hazard 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

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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
Alexander S Belenky et al.
Journal of immunoassay & immunochemistry, 24(3), 311-318 (2003-09-05)
Typical procedure for IgG fragmentation is based on proteolytic cleavage at the hinge region and usually involves a post-digestion purification step. In mice, IgG1 has been found to bind poorly to protein A. As a result, protein G chromatography could
Chui-Liang Chiang et al.
Journal of agricultural and food chemistry, 53(19), 7579-7585 (2005-09-15)
A chitosanolytic enzyme was purified from a commercial ficin preparation by affinity chromatographic removal of cysteine protease on pHMB-Sepharose 4B and cystatin-Sepharose 4B and gel filtration on Superdex 75 HR. The purified enzyme exhibited both chitinase and chitosanase activities, as
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
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

Protocols

This procedure may be used for all Ficin products.

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