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Your Position: > Protein > Cathepsin B > CTB-H5222

Human Cathepsin B / CTSB Protein, His Tag (active enzyme, MALS verified)

  • Synonym
    CTSB,CPSB,APPS
  • Source
    Human Cathepsin B, His Tag(CTB-H5222) is expressed from human 293 cells (HEK293). It contains AA Arg 18 - Ile 339 (Accession # P07858-1 (L26V)).
    Predicted N-terminus: Arg 18 & Leu 80
  • Molecular Characterization
    Cathepsin B Structure

    This protein carries a polyhistidine tag at the C-terminus.

    The Human Cathepsin B will be further processed into mature form (Leu 80-Ile 339). The protein has a calculated MW of 36.7 kDa (pro-form) and 29.5 kDa (mature-form). The protein migrates as 42-50 kDa and 34 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >95% as determined by SDS-PAGE.

    >90% as determined by SEC-MALS.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, pH8.0 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
Cathepsin B SDS-PAGE

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

SEC-MALS
Cathepsin B MALS images

The purity of Human Cathepsin B, His Tag (Cat. No. CTB-H5222) is more than 90% and the molecular weight of this protein is around 60-75 kDa verified by SEC-MALS.

Bioactivity

Measured by its ability to cleave the fluorogenic peptide substrate Z-LR-AMC. The specific activity is >2,500 pmol/min/µg, as measured under the described conditions (QC tested).

  • Background
    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.
  • Clinical and Translational Updates

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