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Cathepsin F (human), (recombinant)

Highly active
 
BML-SE568-0005 5 µg 372.00 USD
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Product Specification

MW:~39kDa
 
Source:Produced in insect cells (secreted) as untagged proenzyme; activated during purification.
 
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.
 

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;

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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