|Calculated MW||This protein is fused with a 6×His tag at the C-terminus, has a calculated MW of 36.7 kDa (Pro) and 29 kDa (Mature). The predicted N-terminus is Arg18 (pro) or Phe74 (mature). DTT-reduced Protein migrates as 43 kDa and 34 kDa due to glycosylation.|
|Other Names||CTSB, CPSB, APPS|
|Results||Measured by its ability to cleave the fluorogenic peptide substrate Z-LR-AMC. Measured in 100 µl reaction mixture containing 25 mM MES, pH 5.0, 0.01 µg rhCathepsin B, and 10 µM reaction substrate. The specific activity is >2800 pmol/min/ µg.|
|Application Notes||Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 µg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.|
|Storage||-20°C; Lyophilized from 0.22 µm filtered solution in 50 mM Tris-HCl and 150 mM NaCl, pH 8.0. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.|
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Provided below are standard protocols that you may find useful for product applications.
Cathepsin B (CTSB) also known as APP secretase (APPS) and CPSB, is an enzymatic protein belonging to the peptidase C1 family. Cathepsin B / CTSB is synthesized as a preproenzyme. Following removal of the signal peptide, the inactive proenzyme undergoes further modifications including removal of the pro region to result in the active enzyme. The catalytic activity of Cathepsin B / APPS contains: Hydrolysis of proteins with broad specificity for peptide bonds; preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L); In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides. As a thiol protease, cathepsin B / CPSB is believed to participate in intracellular degradation and turnover of proteins and has also been implicated in tumor invasion and metastasis. Overexpression of cathepsin B has been associated with esophageal adenocarcinoma and other tumors.
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Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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