Procathepsin E/ Cathepsin E, human recombinant

≥90% Pure Active Human recombinant Procathepsin E/Cathepsin E, an intracellular aspartyl protease.
Catalog #: 7842 | abID:

Product Details

Alternate Name CTSE, Cathepsin E, Procathepsin E
Gene Symbol CTSE
Gene ID 1510
Accession # P14091
Source E. coli
Appearance Lyophilized
Physical Form Description Lyophilized from 5 mg/ml solution in a proprietary buffer
Molecular Weight 43.6 kDa (20-401 aa + N-terminal polyhistidine tag)
Purity by SDS-PAGE ≥90%
Biological Activity BioVision’s Procathepsin E/ Cathepsin E has a specific activity of >500 mU/mg. The Procathepsin E is auto activated to form Cathepsin E after reconstitution. BioVision’s Procathepsin E/ Cathepsin E protein is more stable than a mixture of these proteins m
Reconstitution Instructions Reconstitute with water to 0.5-1 mg/ml. Aliquot and store at –20°C. Avoid repeated freezing and thawing cycles.
Amino Acid Sequence 20-401 aa
Handling Centrifuge the vial prior to opening.
Storage Conditions -20°C
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not to be used in humans


Cathepsin E (EC: (CTSE) is an intracellular gastric aspartyl protease. It was originally identified as a cathepsin D-like acid protease. It is active in acidic conditions in a pH range from 2.5 to 5.5. In vitro experiments have identified several CTSE substrates including insulin beta chain, neurokinin, and FGF. Although the function of CTSE is not completely understood, it has been implicated in several physiological and pathological processes. CTSE is required for antigen presentation on class II MHC molecules. CTSE-deficient macrophages show abnormalities such as autophagy. Like many other cathepsins, CTSE has emerged as a therapy target for cancers, such as pancreatic ductal adenocarcinoma (PDAC). In addition to PDAC, CTSE is also overexpressed in gastric carcinomas and cervical and lung adenocarcinomas. The possible involvement of CTSE in neurodegeneration has also been reported. This protease has a specificity similar to that of pepsin A and cathepsin D. It is found in highest concentration in the surface of epithelial mucus-producing cells of the stomach. It is found in more than half of gastric cancers.

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