SRP6561
Cathepsin K Active human
recombinant, expressed in E. coli, ≥90% (SDS-PAGE)
Synonym(s):
CTSK, CTSO, CTSO3
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.32
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biological source
human
recombinant
expressed in E. coli
Assay
≥90% (SDS-PAGE)
form
liquid
mol wt
23.5 kDa (115-329 aa)
packaging
pkg of 5 μg
pkg of 50 μg
concentration
0.5 mg/mL
technique(s)
activity assay: suitable
suitability
suitable for molecular biology
UniProt accession no.
application(s)
life science and biopharma
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... CTSK(1513)
General description
Cathepsin K is expressed as procathepsin K, which is the inactive proenzyme of cathepsin K. Cathepsin K is a lysosomal cysteine protease and part of the papain cysteine protease family. It is expressed in osteoclasts. The gene encoding this protein is localized on human chromosome 1q21.
Biochem/physiol Actions
Cathepsin K has a role in bone resorption and remodeling. It has a triple helical collagen hydrolase activity. Mutations in the gene encoding this protein have been linked to pycnodysostosis.
Physical form
0.5 mg/mL solution in 25 mM Na2HPO4 and 500 mM NaCl (pH 7.0) with 50% glycerol.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Cathepsin K as a biomarker of bone involvement in type 1 Gaucher disease.
Bobillo L J, et al.
Medicina clinica, 145(7), 281-287 (2015)
Familial pycnodysostosis: identification of a novel mutation in the CTSK gene (cathepsin K).
Toral-Lopez J, et al.
Journal of Investigative Medicine, 59(2), 277-280 (2011)
Diana J Leeming et al.
BMC cancer, 8, 180-180 (2008-07-01)
Breast and prostate cancer patients often develop lesions of locally high bone turnover, when the primary tumor metastasizes to the bone causing an abnormal high bone resorption at this site. The objective of the present study was to determine whether
Increased Circulating Cathepsin K in Patients with Chronic Heart Failure.
Zhao G, et al.
PLoS ONE, 10(8), e0136093-e0136093 (2015)
Andrew Wieczorek et al.
BMC biotechnology, 15, 112-112 (2015-12-17)
Triple helical collagens are the most abundant structural protein in vertebrates and are widely used as biomaterials for a variety of applications including drug delivery and cellular and tissue engineering. In these applications, the mechanics of this hierarchically structured protein
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