Skip to Content
Merck
All Photos(1)

Documents

F4125

Sigma-Aldrich

Ficin from fig tree latex

saline suspension, ≥1.0 units/mg protein (biuret)

Synonym(s):

Debricin, Ficain, higueroxyl delabarre

Sign Into View Organizational & Contract Pricing


About This Item

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

biological source

fig tree (latex)

form

saline suspension

specific activity

≥1.0 units/mg protein (biuret)

mol wt

23.8 kDa

storage temp.

2-8°C

Looking for similar products? Visit Product Comparison Guide

General description

Ficin from fig tree latex exists in multiple isoforms. The isoforms are prone to autolysis at varying temperature and tend to degrade during long term storage. It is a sulfhydryl protease with eight cysteine residues and is stabilized by three disulfide bridges.
Extinction Coefficient: E1% = 21.0 (280 nm)
pI: 9.0

Application

Ficin from fig tree latex has been used:
  • in the electron paramagnetic resonance (EPR) and steady-kinetic measurements for assessing its peroxidase functionality
  • for the digestion of eye tissue sections prior to immunostaining and immunofluorescence

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).

Physical form

Suspension in 2.0 M NaCl and 0.03 M cysteine, pH 5.0

Preparation Note

2× Crystallized

inhibitor

Product No.
Description
Pricing

substrate

Product No.
Description
Pricing

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, 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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Transgenic expression of leukemia inhibitory factor (LIF) blocks normal vascular development but not pathological neovascularization in the eye
Ash J, et al.
Molecular Vision, 11, 298-308 (2005)
Purification and autolysis of the ficin isoforms from fig (Ficus carica cv. Sabz) latex
Zare H, et al.
Phytochemistry, 87, 16-22 (2013)
Lens-specific VEGF-A expression induces angioblast migration and proliferation and stimulates angiogenic remodeling
Ash JD and Overbeek PA
Developmental Biology, 223(2), 383-398 (2000)
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
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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service