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Cathepsin K (human), (recombinant)

Highly active cysteine protease
 
BML-SE553-0010 10 µg 402.00 USD
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Product Specification

Alternative Name:Cathepsin O, Cathepsin O2
 
MW:~26kDa
 
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.
 
EC:3.4.22.38
 
UniProt ID:P43235
 
Concentration:0.023mg/ml
 
Formulation:Liquid. In 50mM sodium acetate, pH 5.5, containing 50mM sodium chloride, 0.5mM EDTA and 5mM DTT.
 
Purity:≥95% (SDS-PAGE)
 
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.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Use/Stability:Stable for at least 6 months after receipt when stored at -80°C.
 
Handling:Keep on dry ice. Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
 
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.
 
BML-SE553 SDS-PAGE
SDS-PAGE Analysis. Lane 1: MW Marker, Lane 2: 1 µg, Lane 3: 2 µg Cathepsin K
BML-SE553 Activation
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.
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BML-SE553 SDS-PAGE BML-SE553 Activation

Product Literature References

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
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; Full Text
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; Full Text
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; Full Text
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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