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Safety Information

SCP0108

Sigma-Aldrich

Cathepsin B Substrate

≥95% (HPLC), lyophilized

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About This Item

Empirical Formula (Hill Notation):
C26H36N10O6
Molecular Weight:
584.63
UNSPSC Code:
12352204
NACRES:
NA.32

product name

Cathepsin B Substrate, colorimetric,

Assay

≥95% (HPLC)

form

lyophilized

composition

Peptide Content, ≥80%

storage condition

protect from light

storage temp.

−20°C

Amino Acid Sequence

Z-Arg-Arg-pNA

General description

Cathepsin B, a bilobal protein, belongs to the papain-like family of cysteine proteases. It is produced as a preproenzyme. Its catalytic site is present at the interface between the two lobes. Cathepsin B has an occluding loop. It is located in the secretory vesicles of the neuronal cells. Active cathepsin B is found in the endosomal or lysosomal compartment under normal physiological conditions.

Biochem/physiol Actions

Cathepsin B is a lysosomal cysteine proteinase that metabolizes important molecules such as β-amyloid precursor protein into harmless fragments. Cathepsin B may be detected using the chromogenic substrate Z-Arg-Arg-pNA (z-arg-arg-p-nitroanalide) or flourogenic substrate Z-Arg-Arg-AMC (z-Arg-Arg-amino-4-methylcoumarin).
Cathepsin B possesses endopeptidase and exopeptidase activity. Active cathepsin B is mostly engaged in intracellular and extracellular protein turnover, which helps cells maintain homeostatic metabolic activity. It also participates in the regulation of pro-hormone and pro-enzyme activation, antigen processing, inflammatory reactions against antigens, tissue remodeling, and apoptosis. Cathepsin B plays a key role in acute pancreatitis. It also plays a vital role in lipid metabolism in atherosclerosis.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

SCP0108-10MG:

Certificates of Analysis (COA)

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Cathepsin B: Basis Sequence: Mouse.
Dora Cavallo-Medved et al.
The AFCS-nature molecule pages, 2011 (2011-01-01)
S Hasnain et al.
The Journal of biological chemistry, 268(1), 235-240 (1993-01-05)
The pH dependence of cathepsin B-catalyzed hydrolyzes is very complex. At least seven dissociable groups are involved in the binding and hydrolysis of 7-amido-4-methyl coumarin and p-nitroaniline (pNA)-based substrates containing a P1 Arg and either a Phe or Arg at
Yasuhito Sako et al.
Experimental parasitology, 127(3), 693-701 (2010-11-26)
Cysteine peptidases have potent activities in the pathogenesis of various parasitic infections, and are considered as targets for chemotherapy and antigens for vaccine. In this study, two cathepsin B-like cysteine peptidases (EmCBP1 and EmCBP2) from Echinococcus multilocularis metacestodes were identified
Ilaria Giusti et al.
Neoplasia (New York, N.Y.), 10(5), 481-488 (2008-05-14)
Vesicles shed by cancer cells are known to mediate several tumor-host interactions. Tumor microenvironment may, in turn, influence the release and the activity of tumor-shed microvesicles. In this study, we investigated the molecular mediators of the pH-dependent proinvasive activity of
Angela J Eykelbosh et al.
Comparative biochemistry and physiology. Part A, Molecular & integrative physiology, 156(2), 218-223 (2010-02-23)
This study presents evidence that cathepsin B, a lysosomal protease, may be involved in the regulation of apoptosis during serum-starvation in teleost follicles. Zebrafish vitellogenic follicles were isolated, incubated under serum-free conditions and homogenized. The follicle extracts demonstrated caspase-3-like activity

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