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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.

Sinônimo(s):

Cathepsin B, Human Liver, cat B, cysteine cathepsin

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About This Item

Número CAS:
Número da licença da enzima:
Código UNSPSC:
12352202
NACRES:
NA.77

fonte biológica

human liver

Nível de qualidade

Ensaio

≥95% (SDS-PAGE)

forma

liquid

atividade específica

≥10 units/mg protein

purificado por

affinity chromatography

fabricante/nome comercial

Calbiochem®

condição de armazenamento

OK to freeze
avoid repeated freeze/thaw cycles

técnica(s)

activity assay: suitable

adequação

suitable for molecular biology

aplicação(ões)

life science and biopharma

Condições de expedição

wet ice

temperatura de armazenamento

−70°C

Informações sobre genes

human ... CTSB(1508)

Descrição geral

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.

Aplicação

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.

Ações bioquímicas/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.

Advertência

Toxicity: Standard Handling (A)

Definição da unidade

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 preparo

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

Reconstituição

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

Outras 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.

Informações legais

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

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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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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