We use cookies to understand how you use our site and to improve the overall user experience. This includes
personalizing content and advertising. Read our Privacy Policy
Recombinant Human Cathepsin E is produced with our mammalian expression system in human cells. The target protein is expressed with sequence (Ser20-Pro396) of Human CTSE fused with a polyhistidine tag at the C-terminus.
Cathepsin E (CTSE) is a gastric aspartyl protease that functions as a disulfide-linked homodimer. It is a member of the Peptidase C1 family, and has a specificity similar to that of Pepsin A and Cathepsin D. CTSE is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome. It is expressed abundantly in the stomach, the Clara cells of the lung and activated B-lymphocytes, and at lower levels in lymph nodes, skin and spleen. CTSE is an intracellular proteinase that have a role in immune function, activation-induced lymphocyte depletion in the thymus, neuronal degeneration and glial cell activation in the brain. Futhermore, it probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation.
Form :
Lyophilized from a 0.2 μM filtered solution of 20mM MES, 150mM NaCl, pH 5.5.
Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.
Storage :
Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
Reconstitution :
Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 μg/ml. Dissolve the lyophilized protein in 1X PBS. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Publications :
Chemoproteomic profiling reveals that cathepsin D off-target activity drives ocular toxicity of β-secretase inhibitors (2016)
