Product Details
| Alternative Name: | Cathepsin O, Cathepsin O2 |
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| MW: | ~26kDa |
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| Source: | Produced in insect cells. Purified as full-length proenzyme (see Prod. No. BML-SE367), then auto-activated at low pH. Produced in a baculovirus expression system. |
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| EC: | 3.4.22.38 |
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| UniProt ID: | P43235 |
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| Formulation: | Liquid. In 50mM sodium acetate, pH 5.5, containing 50mM sodium chloride, 0.5mM EDTA and 5mM DTT. |
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| Purity: | ≥95% (SDS-PAGE) |
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| Specific Activity: | ≥1.5 U/mg. One unit hydrolyzes 1µmol Z-Phe-Arg-AMC substrate (OMNICATHEPSIN® Fluorogenic Substrate, Prod. No. BML-P139) per min. at 37°C. |
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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 at -80°C. |
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| Handling: | Keep on dry ice. Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C. |
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| Scientific Background: | 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 osteoporosis, atherosclerosis, arthritis, and pycnodysostosis. |
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| Regulatory Status: | RUO - Research Use Only |
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Activation of ProCathepsin K. Lanes 2-7 each contain 1 µg of total protein during time-course activation at low pH. Lane 2: pre-activation, Lane 3: 0 min, Lane 4: 1 hr, Lane 5: 2 hr, Lane 6: 3 hr, Lane 7: 4 hr.
SDS-PAGE Analysis. Lane 1: MW Marker, Lane 2: 1 µg, Lane 3: 2 µg Cathepsin K
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Product Literature References
Mechanical strain modulates extracellular matrix degradation and byproducts in an isoform-specific manner: A. Yeganegi, et al.; Biochim. Biophys. Acta Gen. Subj.
1867, 130286 (2023),
Abstract;
Potential benefit of the cathepsin S inhibitor, ASP1617, as a treatment for systemic lupus erythematosus: Y. Kawato, et al.; Eur. J. Pharmacol.
919, 174826 (2022),
Abstract;
Two Tags in One Probe: Combining Fluorescence- and Biotin-based Detection of the Trypanosomal Cysteine Protease Rhodesain: C. Lemke, et al.; Chemistry
28, e202201636 (2022),
Abstract;
A Clinical-Stage Cysteine Protease Inhibitor blocks SARS-CoV-2 Infection of Human and Monkey Cells: D.M. Mellott, et al.; ACS Chem. Biol.
16, 642 (2021),
Abstract;
Full Text
Cell penetrable, clickable and tagless activity-based probe of human cathepsin L: D. Dana, et al.; Bioorg. Chem.
85, 505 (2019),
Application(s): Activity assay,
Abstract;
A type VII collagen subdomain mutant is thermolabile and shows enhanced proteolytic degradability - Implications for the pathogenesis of recessive dystrophic epidermolysis bullosa?: C. Windler, et al.; Biochim. Biophys. Acta Mol. Basis Dis.
1863, 52 (2017),
Abstract;
Unexpected Activity of a Novel Kunitz-type Inhibitor: INHIBITION OF CYSTEINE PROTEASES BUT NOT SERINE PROTEASES: D. Smith, et al.; J. Biol. Chem.
291, 19220 (2016),
Abstract;
Full Text
Matrix-metalloproteinase-9 is cleaved and activated by cathepsin K: J. Christensen, et al.; BMC Res. Notes
8, 322 (2015),
Abstract;
Full Text
Over-expression of cystatin C in synovium does not reduce synovitis or cartilage degradation in established osteoarthritis: S. Kyostio-Moore, et al.; Arthritis. Res. Ther.
17, 5 (2015),
Application(s): Western Blotting,
Abstract;
Full Text
Development of a highly potent, selective, and cell-active Inhibitor of cysteine cathepsin L-A hybrid design approach: D. Dana, et al.; Chem. Commun. (Camb.)
50, 10875 (2014),
Abstract;
Cathepsin S Cannibalism of Cathepsin K as a Mechanism to Reduce Type I Collagen Degradation: Z.T. Barry, et al. ; J. Biol. Chem.
287, 27723 (2012),
Application(s): Fluorescent Assay ,
Abstract;
Full Text
Manipulating substrate and pH in zymogr aphy protocols selectively distinguishes cathepsins K, L, S, and V activity in cells and tissues: C.L. Wilder, et al.; Arch. Biochem. Biophys.
516, 52 (2011),
Application(s): Western Blot,
Abstract;
Full Text
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;
Full Text
Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages: Y. Yasuda, et al.; J. Biol. Chem.
279, 36761 (2004),
Abstract;
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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;
Cathepsin K--a marker of macrophage differentiation?: F. Bühling, et al.; J. Pathol.
195, 375 (2001),
Abstract;
The collagenolytic activity of cathepsin K is unique among mammalian proteinases: P. Garnero, et al.; J. Biol. Chem.
273, 32347 (1998),
Abstract;
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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;
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Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency: B.D. Gelb, et al.; Science
273, 1236 (1996),
Abstract;
The baculovirus cysteine protease has a cathepsin B-like S2-subsite specificity: D. Brömme & K. Okamoto; Biol. Chem. Hoppe Seyler
376, 611 (1995),
Abstract;
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