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.
Sinónimos:
Cathepsin B, Human Liver, cat B, cysteine cathepsin
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About This Item
Número de CAS:
Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.77
Productos recomendados
origen biológico
human liver
Nivel de calidad
descripción
Merck USA index - 14, 1905
Ensayo
≥95% (SDS-PAGE)
Formulario
liquid
actividad específica
≥10 units/mg protein
purificado por
affinity chromatography
fabricante / nombre comercial
Calbiochem®
condiciones de almacenamiento
OK to freeze
avoid repeated freeze/thaw cycles
técnicas
activity assay: suitable
idoneidad
suitable for molecular biology
aplicaciones
life science and biopharma
Condiciones de envío
wet ice
temp. de almacenamiento
−70°C
Información sobre el gen
human ... CTSB(1508)
Descripción general
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.
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.
Aplicación
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.
Acciones bioquímicas o fisiológicas
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.
Advertencia
Toxicity: Standard Handling (A)
Definición de unidad
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.
Forma física
In 50 mM sodium acetate buffer, 1 mM EDTA, pH 5.0.
Nota de preparación
Prepared from tissues of individuals that have been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
Reconstitución
Following initial thaw, aliquot and freeze (-70°C).
Otras notas
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.
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.
Información legal
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Certificados de análisis (COA)
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Cathepsin B: Basis Sequence: Mouse
Cavallo-Medved D, et al.
The AFCS-nature Molecule Pages (2011)
Zsanett Jancsó et al.
Gastroenterology, 158(4), 1083-1094 (2019-11-22)
Mutations in the human serine protease 1 gene (PRSS1), which encodes cationic trypsinogen, can accelerate its autoactivation and cause hereditary or sporadic chronic pancreatitis. Disruption of the locus that encodes cationic trypsinogen in mice (T7) causes loss of expression of
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