SCP0108
Cathepsin B Substrate
≥95% (HPLC), lyophilized
Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
About This Item
Doporučené produkty
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
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Osvědčení o analýze (COA)
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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
Cathepsin B: Basis Sequence: Mouse.
The AFCS-nature molecule pages, 2011 (2011-01-01)
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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
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