SRP0292
Cathepsin S Active human
recombinant, expressed in FreeStyle™ 293-F cells, ≥90% (SDS-PAGE)
Synonym(s):
MGC3886
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About This Item
UNSPSC Code:
12352204
NACRES:
NA.54
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recombinant
expressed in FreeStyle™ 293-F cells
Assay
≥90% (SDS-PAGE)
form
aqueous solution
specific activity
≥8100 pmol/min-μg
mol wt
37 kDa
NCBI accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... CTSS(1520)
General description
Human cathepsin S (GenBank Accession No. NM_004079.3), CD33 signal peptide(amino acids 1-16) + cathepsin S (amino acids 17-331), with C-terminal HIS tag, MW = 37 kDa, expressed in FreeStyle 293-F cells.
Application
Active human cathepsin S is useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling. Active human cathepsin S has been used in a study to assess the pathogenesis of Alzheimer′s disease. Active human cathepsin S has also been used in a study to investigate the optimization of selectivity of Azepanone-based inhibitors.
Unit Definition
One unit is defined as the amount of enzyme that will cleave 1 pmol of substrate per min at 37°C
Physical form
Formulated in 45 mM Tris-HCl, pH 8.0, 124 mM NaCl, 2.4 mM KCl, 225 mM imidazole, 3 mM DTT, and 10% glycerol.
Preparation Note
Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.
Legal Information
FreeStyle is a trademark of Invitrogen Corp.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
Storage Class Code
6.1C - Combustible, acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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D Brömme et al.
Protein science : a publication of the Protein Society, 5(4), 789-791 (1996-04-01)
We have expressed active human cathepsin S to 60 mg/L in Sf9 cells using a baculovirus system. Production of milligram quantities has facilitated crystallographic studies to determine the structure of this enzyme, which has unique properties among lysosomal cysteine proteinases.
Azepanone-based inhibitors of human cathepsin S: optimization of selectivity via the P2 substituent.
Jeffrey K Kerns et al.
Bioorganic & medicinal chemistry letters, 21(15), 4409-4415 (2011-07-08)
A series of azepanone inhibitors of cathepsin S is described. Selectivity over both cathepsin K and cathepsin L was achieved by varying the P2 substituent. Ultimately, a balanced potency and selectivity profile was achieved in compound 39 possessing a 1-methylcyclohexyl
Harry Pantazopoulos et al.
eNeuro, 7(4) (2020-07-29)
Perineuronal nets (PNNs) are extracellular matrix (ECM) structures that envelop neurons and regulate synaptic functions. Long thought to be stable structures, PNNs have been recently shown to respond dynamically during learning, potentially regulating the formation of new synapses. We postulated
Israel Schechter et al.
Biological chemistry, 392(6), 555-569 (2011-05-19)
β-site APP-cleaving enzyme (BACE1) cleaves the wild type (WT) β-site very slowly (k(cat)/K(m): 46.6 m(-1) s(-1)). Therefore we searched for additional β-secretases and identified three cathepsins that split the WT β-site much faster. Human cathepsin S cleaves the WT β-site
Haiying Jiang et al.
Nature communications, 5, 3838-3838 (2014-06-05)
Cysteine proteases play important roles in pathobiology. Here we reveal that cathepsin K (CatK) has a role in ischaemia-induced neovascularization. Femoral artery ligation-induced ischaemia in mice increases CatK expression and activity, and CatK-deficient mice show impaired functional recovery following hindlimb
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