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 United States

Procathepsin K (human), (recombinant)

 
BML-SE367-0010 10 µg 265.00 USD
 

Recombinant glycosylated procathepsin K (also known as cathepsin O or cathepsin O2) cloned from human cDNA, expressed in insect cells, and purified as full-length proenzyme. Cathepsin K, a member of the papain family of cysteine proteases, acts upon proteins such as collagen, AL amyloid, kinin, and elastin. It is a lysosomal protease expressed primarily in osteoclasts, but also in other cell types such as macrophages. It functions in bone remodeling and is implicated in disease states such as atherosclerosis, arthritis, and pycnodysostosis.

Product Specification

Alternative Name:Cathepsin O
 
MW:35.3kDa
 
Purity:>95% (SDS-PAGE)
 
Source/Host:Produced in insect cells. Full length glycosylated human procathepsin K.
 
Application:Study enzyme kinetics, cleave target substrates and screen for inhibitors.
 
Long Term Storage:-80°C
 
Use/Stability:-80°C. After initial defrost, aliquot product into individual tubes and refreeze at -80°C. Avoid repeated freeze/defrost cycles and extended periods unfrozen. This enzyme is stable when stored as received under the above conditions. Procedures such as dilution of the enzme followed by refreezing could lead to loss of activity.
 
Handling:After opening, prepare aliquots and store at -80°C.
Avoid freeze/thaw cycles.
 
Miscellaneous/General:Cathepsin K, a member of the papain family of cysteine proteases, acts upon proteins such as collagen, AL amyloid, kinin and elastin. It is a lysosomal protease expressed primarily in osteoclasts, but also in other cell types such as macrophages. It functions in bone remodeling and is implicated in disease states such as atherosclerosis, arthritis and pycnodysostosis.
 
Background / Technical Information:Please click here for the comprehensive product datasheet.
 
BML-SE367 SDS-PAGE
SDS-PAGE Analysis: Lane 1: MWM; Lane 2: 1.0 µg of purified Procathepsin K; Lane 3: 1.0 µg Cathepsin K after activation at low pH for 3 hours.
BML-SE367 AA
Activation of procathepsin K at 22°C. Lane 1, size marker. Lane 2, 0.5 hour. Lane 3, 1 hour. Lane 4, 2 hours. Lane 5, 3 hours. Lane 6, 4 hours. 1 ug per lane, loaded after EtOH precipitation/wash and resuspension in SDS-PAGE sample buffer.
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BML-SE367 SDS-PAGE BML-SE367 AA

General Literature References

Cathepsin K-dependent toll-like receptor 9 signaling revealed in experimental arthritis.: M. Asagiri et al.; Science 319, 624 (2008), Abstract;
Cathepsin K: a cysteine protease with unique kinin-degrading properties.: E. Godat et al.; Biochem. J. 383, 501 (2004), Abstract;
Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages.: Y. Yasuda et al.; J. Biol. Chem. 279, 36761 (2004), Abstract;
Cleavage of AL amyloid proteins and AL amyloid deposits by cathepsins B, K, and L.: S. Bohne et al.; J. Pathol. 203, 528 (2004), Abstract;
Design of noncovalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides.: S.F. Chowdhury et al.; J. Med. Chem. 45, 5321 (2002), Abstract;
Cathepsin K--a marker of macrophage differentiation?: F. Buhling et al.; J. Pathol. 195, 375 (2001), Abstract;
Interdependency of sequence and positional specificities for cysteine proteases of the papain family.: D.K. Nagler et al.; Biochemistry 38, 4868 (1999), Abstract;
The collagenolytic activity of cathepsin K is unique among mammalian proteinases.: P. Garnero et al.; J. Biol. Chem. 273, 32347 (1998), Abstract;
Major increase in endopeptidase activity of human cathepsin B upon removal of occluding loop contacts.: D.K. Nagler et al.; Biochemistry 36, 12608 (1997), Abstract;
Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts.: F.H. Drake et al.; J. Biol. Chem. 271, 12511 (1996), Abstract;
Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency.: B.D. Gelb et al.; Science 273, 1236 (1996), Abstract;
Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution.: D. Bromme & K. Okamoto; Biol. Chem. Hoppe Seyler 376, 379 (1995), Abstract;
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