F4165
Ficin from fig tree latex
powder, ≥0.1 unit/mg solid
Synonym(s):
Debricin, Ficain, higueroxyl delabarre
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
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
Looking for similar products? Visit Product Comparison Guide
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
Product No.
Description
Pricing
substrate
Product No.
Description
Pricing
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
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.
Customers Also Viewed
Robertson D Davenport et al.
Transfusion, 44(6), 849-852 (2004-05-26)
Cefotetan can cause severe immune hemolytic anemia that may persist long after the drug is discontinued. To study the binding of cefotetan to RBCs, patients who received cefotetan were followed and tested for the presence of antibody to cefotetan. Patients
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
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
Sadami Ohtsubo et al.
Journal of agricultural and food chemistry, 53(13), 5218-5224 (2005-06-23)
On the basis of cDNA sequences, we found that the calli of rice encodes an amino acid sequence that shares 56% and 89% identity, respectively, with oryzacystatin-I and oryzacystatin-II. This sequence differs from that of oryzacystatin-II in the N-terminal region
J D Reid et al.
The Biochemical journal, 357(Pt 2), 343-352 (2001-07-06)
The possibility of a slow post-acylation conformational change during catalysis by cysteine proteinases was investigated by using a new chromogenic substrate, N-acetyl-Phe-Gly methyl thionoester, four natural variants (papain, caricain, actinidin and ficin), and stopped-flow spectral analysis to monitor the pre-steady
Protocols
This procedure may be used for all Ficin products.
This procedure may be used for all Ficin products.
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