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Cathepsin F (human), (recombinant)

Highly active
 
BML-SE568-0005 5 µg 401.00 USD
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Product Specification

MW:~39kDa
 
Source:Produced in insect cells (secreted) as untagged proenzyme; activated during purification. Produced in a baculovirus expression system.
 
EC:3.4.22.41
 
UniProt ID:Q9UBX1
 
Formulation:Liquid. In 20mM NaOAc, pH 5.0, containing 2.5mM EDTA, 250mM sodium chloride and 20mM L-cysteine.
 
Purity:≥80% (SDS-PAGE)
 
Purity Detail:Purified by multi-step chromatography.
 
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.
 
Application Notes:Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Use/Stability:Stable for at least 6 months after receipt when stored as supplied at -80°C.
 
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
 
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.
 
Regulatory Status:RUO - Research Use Only
 

Product Literature References

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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