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Key Documents

SRP0292

Sigma-Aldrich

Cathepsin S Active human

recombinant, expressed in FreeStyle 293-F cells, ≥90% (SDS-PAGE)

Synonyme(s) :

CTSS, MGC3886

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About This Item

Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

human

Produit recombinant

expressed in FreeStyle 293-F cells

Pureté

≥90% (SDS-PAGE)

Forme

aqueous solution

Activité spécifique

≥8100 pmol/min-μg

Poids mol.

37 kDa

Technique(s)

activity assay: suitable

Adéquation

suitable for molecular biology

Numéro d'accès NCBI

Application(s)

life science and biopharma

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... CTSS(1520)

Description générale

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.

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.

Actions biochimiques/physiologiques

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.

Définition de l'unité

One unit is defined as the amount of enzyme that will cleave 1 pmol of substrate per min at 37°C

Forme physique

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.

Notes préparatoires

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.

Informations légales

FreeStyle is a trademark of Invitrogen Corp.

Pictogrammes

Health hazardExclamation mark

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2

Code de la classe de stockage

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

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.
Richard D A Wilkinson et al.
Biological chemistry, 396(8), 867-882 (2015-04-16)
Cathepsin S is a member of the cysteine cathepsin protease family. It is a lysosomal protease which can promote degradation of damaged or unwanted proteins in the endo-lysosomal pathway. Additionally, it has more specific roles such as MHC class II
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

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