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製品名
カテプシンB基質、比色分析,
アッセイ
≥95% (HPLC)
フォーム
lyophilized
組成
Peptide Content, ≥80%
保管条件
protect from light
保管温度
−20°C
Amino Acid Sequence
Z-Arg-Arg-pNA
詳細
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.
生物化学的／生理学的作用
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.
保管分類コード
11 - Combustible Solids
WGK
WGK 3
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
SCP0108-10MG:
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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
Cathepsin B: Basis Sequence: Mouse.
Dora Cavallo-Medved et al.
The AFCS-nature molecule pages, 2011 (2011-01-01)
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
Xiaohua Peng et al.
Journal of immunology (Baltimore, Md. : 1950), 209(7), 1314-1322 (2022-09-28)
Postviral bacterial infections are a major health care challenge in coronavirus infections, including COVID-19; however, the coronavirus-specific mechanisms of increased host susceptibility to secondary infections remain unknown. In humans, coronaviruses, including SARS-CoV-2, infect lung immune cells, including alveolar macrophages, a
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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