F4165
Ficin from fig tree latex
powder, ≥0.1 unit/mg solid
Synonym(s):
Debricin, Ficain, higueroxyl delabarre
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1000 UNITS
$141.00
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1000 UNITS
$141.00
About This Item
$141.00
PRICE WITHOUT NATIONAL TAXES
Check Cart for Availability
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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
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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
K B Devaraj et al.
International journal of biological macromolecules, 45(3), 248-254 (2009-06-02)
Effect of pH on the conformational behaviour of ficin (EC 3.4.22.3), a cysteine protease from the latex of Ficus carica was monitored by circular dichroism, fluorescence spectroscopy, ANS binding and hydrodynamic studies. The results obtained from near- and far-UV CD
A Saito et al.
Biochemistry and molecular biology international, 46(1), 27-34 (1998-10-24)
Amino acid sequencing of the ficin-derived C-terminal fragments of alpha-1-antiproteinase (also called alpha-1-antitrypsin or alpha-1-proteinase inhibitor) prepared from rabbit plasma revealed the presence of the E isoform, which had been confirmed in the cDNA library in addition to the F
V B Reddy et al.
The British journal of dermatology, 163(3), 532-535 (2010-05-25)
Bromelain, ficin and papain are cysteine proteases from plants that produce itch upon injection into skin. Their mechanism of action has not been considered previously. To determine the mechanism by which these proteases function. The ability of these proteases to
Michèle Himmelspach et al.
Thrombosis and haemostasis, 88(6), 1003-1011 (2003-01-17)
The development of inhibitory antibodies is a serious complication in hemophilic patients, severely compromising therapeutic success. Bleeding episodes in affected patients are controlled by treatment with a plasma-derived prothrombin complex concentrate (PCC), activated PCC (APCC) or recombinant activated factor VII.
Protocols
This procedure may be used for all Ficin products.
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