219362

Cathepsin B, Human Liver

Cathepsin B, Human Liver, CAS 9047-22-7, is a purified native cathepsin B from human liver, purified by affinity chromatography. Upregulated in many types of tumors.

• Synonyme(s) : Cathepsin B, Human Liver, cat B, cysteine cathepsin
• Numéro CAS: 9047-22-7
• Numéro de classification (Commission des enzymes): 3.4.22.1 (BRENDA, IUBMB)
• Code UNSPSC : 12352202
• Nomenclature NACRES : NA.77

Propriétés

• Source biologique: human liver
• Niveau de qualité: 100
• Pureté: ≥95% (SDS-PAGE)
• Forme: liquid
• Activité spécifique: ≥10 units/mg protein
• Produit purifié par: affinity chromatography
• Fabricant/nom de marque: Calbiochem^®
• Conditions de stockage: OK to freeze; avoid repeated freeze/thaw cycles
• Technique(s): activity assay: suitable
• Adéquation: suitable for molecular biology
• Application(s): life science and biopharma
• Conditions d'expédition: wet ice
• Température de stockage: −70°C
• Informations sur le gène: human ... CTSB(1508)

Description

Description générale

Research area: Cell Signaling

Native cathepsin B from human liver, purified by affinity chromatography and HPLC. The most investigated enzyme of all lysosomal cysteine proteases. Cathepsin B belongs to the papain-like family of cysteine proteases and is produced as a preproenzyme. It is a bilobal protein, and its catalytic site is situated at the interface between the two lobes.

Application

Cathepsin B, Human Liver, has been used in:

• Diagnostics: as a potent and independent prognostic marker for endometrial cancer, pancreatic adenocarcinoma, and inflammatory disease.
• Drug development: during the neovascularization process and as a potent therapeutic target for various pathologies, cancer progression, and osteoarthritis in humans.
• Pharmacology: for increasing the therapeutic index of doxorubicin by incorporating the cathepsin B cleavable spacer Phe-Lys-4-aminobenzyloxycarbonyl into an albumin-binding prodrug.
• Molecular biology: in cathepsin B activity assay.

Actions biochimiques/physiologiques

Cathepsin B acts as both endo and exopeptidase. While as an endopeptidase it cleaves amino acids with a large hydrophobic side chain in the P2 site of the protein/peptide substrate, on the other hand as an exopeptidase it eliminates two amino acids (dipeptide) from the C terminus of a polypeptide substrate, thereby categorizing the enzyme as a peptidyl dipeptidase. It maintains homeostatic metabolic activity within cells through regular turnover of both intracellular and extracellular proteins. Additionally, it is involved in various cellular functions like regulation of pro-enzyme and pro-hormone activation, tissue remodeling, antigen processing, apoptosis, and inflammatory responses to antigens. The expression and activity of cathepsin B have been linked to several pathologies, including cardiovascular disease, cancer, Alzheimer’s, arthritis, and pancreatitis. Overexpression of cathepsin B has been observed in brain, breast, gastric, prostate, esophageal, skin, lung, ovarian, colon, and thyroid cancers and correlates positively with their invasive and metastatic capabilities. Cathepsin B is shown to facilitate tumor invasion by dissolving extracellular barriers.

Avertissement

Toxicity: Standard Handling (A)

Définition de l'unité

One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol Z-RR-β-naphthylamide per min at 40°C, using 100 mM Na⁺/K⁺ pH 6.0, with 1.33 mM EDTA and 2 mM DTT as the activation buffer.

Forme physique

In 50 mM sodium acetate buffer, 1 mM EDTA, pH 5.0.

Notes préparatoires

Prepared from tissues of individuals that have been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

Reconstitution

Following initial thaw, aliquot and freeze (-70°C).

Autres remarques

Hirai, K., et al. 1999. Hum. Pathol.30, 680.
Kostoulas, G., et al. 1999. FEBS Lett.455, 286.
Strojnik, T., et al. 1999. Clin. Cancer Res.5, 559.
Maquire, T.M., et al. 1998. Int. J. Biol. Markers13, 139.
Berquim, I.M., and Sloane, B.F. 1996. Adv. Exp. Med. Biol.389, 281.

Informations légales

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Informations sur la sécurité

• Code de la classe de stockage: 11 - Combustible Solids
• Classe de danger pour l'eau (WGK): WGK 3
• Point d'éclair (°F): Not applicable
• Point d'éclair (°C): Not applicable