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Human Cathepsin B / CTSB Protein  pdf  pdf  pdf

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Human Cathepsin B / CTSB Protein (Human Cathepsin B, His Tag) Arg 18 - Ile 339 (Accession # NP_001899) was produced in human 293 cells (HEK293) at ACROBiosystems.

Molecular Characterization

rh CTSB is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 36.7 kDa (pro-form) and 29 kDa (mature-form). The predicted N-terminus is Arg18 (pro-form) or Phe74 (mature-form). Due to glycosylation, The reducing (R) protein migrates as 43 kDa (pro-form) band in SDS-PAGE and there may be a 34 kDa (mature-form) band.


Less than 1.0 EU per μg by the LAL method.


>95% as determined by SDS-PAGE.


Lyophilized from 0.22 μm filtered solution in 50mM Tris-HCl, 150mM NaCl, pH 8.0. Normally Mannitol or Trehalose are added as protectants before lyophilization.

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See Certificate of Analysis for reconstitution instructions and specific concentrations.


Avoid repeated freeze-thaw cycles.

No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C); After reconstitution under sterile conditions for 3 months (-70°C).



Human Cathepsin B / CTSB Protein
Human Cathepsin B, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.



Cathepsin B (CTSB) is 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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