Product Details
| MW: | ~39kDa |
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| Source: | Produced in insect cells (secreted) as untagged proenzyme; activated during purification. Produced in a baculovirus expression system. |
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| EC: | 3.4.22.41 |
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| UniProt ID: | Q9UBX1 |
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| Formulation: | Liquid. In 20mM NaOAc, pH 5.0, containing 2.5mM EDTA, 250mM sodium chloride and 20mM L-cysteine. |
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| Purity: | ≥80% (SDS-PAGE) |
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| Purity Detail: | Purified by multi-step chromatography. |
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| Specific Activity: | ≥1 U/mg. One unit hydrolyzes 1 µmol Z-Phe-Arg-AMC substrate (OMNICATHEPSIN® Fluorogenic Substrate, Prod. No. BML-P139) per min. at 37°C. |
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| Application Notes: | Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Use/Stability: | Stable for at least 6 months after receipt when stored as supplied at -80°C. |
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| Handling: | Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C. |
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| Scientific Background: | Recombinant glycosylated procathepsin F cloned from human cDNA (NM_003793), expressed in insect cells, and purified as the active form of the enzyme. Cathepsin F, a member of the papain family of lysosomal cysteine proteases, acts upon proteins such as MHC Class II-associated invariant chain and ApoB-100. It is inhibited by the cysteine proteinase inhibitor E-64 (Prod. No. BML-EI105) and cystatin C (Prod. No. BML-SE479). It is a lysosomal protease expressed in numerous tissues, notably brain and macrophages. It functions in the immune system and is implicated in disease states such as atherosclerosis, cancer, and angiogenesis. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
An evolutionary molecular adaptation of an unusual stefin from the liver fluke Fasciola hepatica redefines the cystatin superfamily: M. Busa, et al.; J. Biol. Chem.
299, 102970 (2023),
Abstract;
Lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) is a substrate of cathepsin-F, a cysteine protease mutated in type-B-Kufs-disease: J. Peters, et al.; Biochem. Biophys. Res. Commun.
457, 334 (2015),
Application(s): Cell Culture, Western Blotting,
Abstract;
Development of cell-active non-peptidyl inhibitors of cysteine cathepsins: D. Dana, et al.; Bioorg. Med. Chem.
21, 2975 (2013),
Abstract;
General Literature References
Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer: G. Vazquez-Ortiz, et al.; BMC Cancer
5, 164 (2005),
Abstract;
Full Text
Cysteine protease cathepsin F is expressed in human atherosclerotic lesions, is secreted by cultured macrophages and modifies low density lipoprotein particles in vitro: K. Oorni; J. Biol. Chem.
279, 34776 (2004),
Abstract;
Full Text
Human cathepsin F: expression in baculovirus system, characterization and inhibition by protein inhibitors: M. Fonovic, et al. ; Biol. Chem.
385, 505 (2004),
Abstract;
Expression, purification, crystallization and preliminary X-ray diffraction studies of human cathepsin F complexed with irreversible vinyl sulfone inhibitor: J.D. Ho, et al.; Acta Crystallogr. D. Biol. Crystallogr.
D58, 2187 (2002),
Abstract;
The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators: J.R. Somoza, et al.; J. Mol. Biol.
322, 559 (2002),
Abstract;
Human Cathepsins F and W: A new subgroup of cathepsins: T. Wex, et al.; Biochem. Biophys. Res. Commun.
259, 401 (1999),
Abstract;
Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain: I. Santamaria, et al.; J. Biol. Chem.
274, 13800 (1999),
Abstract;
Full Text
Human cathepsin F: Molecular cloning , functional expression, tissue localization, and enzymatic characterization: B. Wang, et al.; J. Biol. Chem.
273, 32000 (1998),
Abstract;
Full Text
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