SRP0292
Cathepsin S Active human
recombinant, expressed in FreeStyle™ 293-F cells, ≥90% (SDS-PAGE)
Synonym(s):
CTSS, MGC3886
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About This Item
UNSPSC Code:
12352204
NACRES:
NA.54
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biological source
human
recombinant
expressed in FreeStyle™ 293-F cells
assay
≥90% (SDS-PAGE)
form
aqueous solution
specific activity
≥8100 pmol/min-μg
mol wt
37 kDa
technique(s)
activity assay: suitable
suitability
suitable for molecular biology
NCBI accession no.
application(s)
life science and biopharma
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... CTSS(1520)
General description
Research area: Cell Signaling
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. Cathepsin S belongs to the cysteine cathepsin protease family. It has limited tissue expression, being associated with antigen-presenting cells localized in lymph and spleen, as well as other immune cells like macrophages. Human cathepsin S is produced from its corresponding CTSS gene on chromosome 1q21 and is synthesized as a pre-proenzyme.
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. Cathepsin S belongs to the cysteine cathepsin protease family. It has limited tissue expression, being associated with antigen-presenting cells localized in lymph and spleen, as well as other immune cells like macrophages. Human cathepsin S is produced from its corresponding CTSS gene on chromosome 1q21 and is synthesized as a pre-proenzyme.
Application
Active human cathepsin S has been used:
- to assess the pathogenesis of Alzheimer′s disease.
- to investigate the optimization of selectivity of Azepanone-based inhibitors.
- for the immunocytochemical detection of cathepsin-S in mouse samples.
- for incubating mouse brain sections to test the impact of cathepsin-S on perineuronal nets (PNNs) integrity.
Biochem/physiol Actions
Cathepsin S, as a lysosomal protease, facilitates the breakdown of unwanted and damaged proteins in the endo-lysosomal pathway. Moreover, it plays specific roles, such as contributing to major histocompatibility complex (MHC) class II antigen presentation by aiding in the degradation of the invariant chain. Dysregulation of cathepsin S has been associated with various pathological conditions, such as cancer, arthritis, and cardiovascular disease. Cathepsin S is useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling. It is also used as a biomarker for atherosclerosis, diabetes, adiposity, and atherogenesis. Moreover, it acts as a promising target against brain-penetrating and for the treatment of multiple sclerosis and neuropathic pain.
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.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
wgk_germany
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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