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Key Documents

F4125

Sigma-Aldrich

Ficin from fig tree latex

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

Synonyme(s) :

Debricin, Ficain, higueroxyl delabarre

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

fig tree (latex)

Forme

saline suspension

Activité spécifique

≥1.0 units/mg protein (biuret)

Poids mol.

23.8 kDa

Température de stockage

2-8°C

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Description générale

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

Actions biochimiques/physiologiques

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.

Définition de l'unité

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).

Forme physique

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

Notes préparatoires

2× Crystallized

Inhibiteur

Réf. du produit
Description
Tarif

Substrat

Réf. du produit
Description
Tarif

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type ABEK (EN14387) respirator filter


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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)
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)
Purification and autolysis of the ficin isoforms from fig (Ficus carica cv. Sabz) latex
Zare H, et al.
Phytochemistry, 87, 16-22 (2013)
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

Protocoles

This procedure may be used for all Ficin products.

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