Procathepsin K (human), (recombinant)

BML-SE367

Revised 05-Mar-10

Procathepsin K (human), (recombinant)
SYNONYMS	Cathepsin O
PRODUCT LINE	Cancer
PRODUCT CATEGORY	Cathepsins

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
BML-SE367-0010		10 µg	257.00 USD

Product Specification

MW:	35.3kDa
SOURCE/HOST:	Produced in insect cells. Full length glycosylated human procathepsin K.
PURITY:	>95% (SDS-PAGE)
APPLICATION:	Study enzyme kinetics, cleave target substrates and screen for inhibitors.
SHIPPING:	SHIPPED ON DRY ICE
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.

Product Images

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Product Description

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.

General Information

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
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General Literature References

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
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
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
The collagenolytic activity of cathepsin K is unique among mammalian proteinases.: P. Garnero et al.; J. Biol. Chem. 273, 32347 (1998) Abstract
Interdependency of sequence and positional specificities for cysteine proteases of the papain family.: D.K. Nagler et al.; Biochemistry 38, 4868 (1999) Abstract
Cathepsin K--a marker of macrophage differentiation?: F. Buhling et al.; J. Pathol. 195, 375 (2001) 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 cysteine protease with unique kinin-degrading properties.: E. Godat et al.; Biochem. J. 383, 501 (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
Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages.: Y. Yasuda et al.; J. Biol. Chem. 279, 36761 (2004) Abstract
Cathepsin K-dependent toll-like receptor 9 signaling revealed in experimental arthritis.: M. Asagiri et al.; Science 319, 624 (2008) Abstract