Mouse Cathepsin B / CTSB Protein, His Tag (Pro-form, MALS verified)

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CTB-M52H9-50ug
$350.00
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CTB-M52H9-1mg (500ug X 2)
$2,380.00
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CTB-M52H9
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Synonyms

CTSB, CPSB, APPS

Source

Mouse Cathepsin B, His Tag (CTB-M52H9) is expressed from human 293 cells (HEK293). It contains AA His 18 - Phe 339 (Accession # P10605-1).

Predicted N-terminus: His 18

Molecular Characterization

This protein carries a polyhistidine tag at the C-terminus. This protein contains an Activation peptide, and will be partially processed into Pro form with calculated MW of 37.3 kDa and mature form with calculated MW of 29 kDa under reducing (R) condition. The protein migrates as 43-47 kDa and 32-35 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

Endotoxin

Less than 1.0 EU per μg by the LAL method / rFC method.

Purity

>90% as determined by SDS-PAGE.

>95% as determined by SEC-MALS.

Formulation

Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, pH7.5 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.

Shipping and Storage

This product is shipped at ambient temperature.

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:
  • -20°C to -70°C for 12 months in lyophilized state;
  • -70°C for 3 months under sterile conditions after reconstitution.

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.