Product Details
| Source: | Isolated from human liver. |
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| UniProt ID: | P07339 |
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| Formulation: | Lyophilized with phosphate buffer. |
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| Purity: | ≥95% (SDS-PAGE) |
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| Application Notes: | Useful for inhibitor screening, kinetic studies, and cleavage of substrates in vitro or in tissue culture. |
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| Reconstitution: | Reconstitute just before first use with original volume of water. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Handling: | Avoid freeze/thaw cycles. After reconstitution, prepare aliquots and store at -80°C. |
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| Scientific Background: | Cathepsin D is a lysosomal protease that can also be secreted from the cell and is involved in protein degradation, apoptosis, and cancer. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Cathepsin D regulates cerebral Aβ42/40 ratios via differential degradation of Aβ42 and Aβ40: C.N. Suire, et al.; Alzheimers Res. Ther.
12, 80 (2020),
Abstract;
Full Text
Cell penetrable, clickable and tagless activity-based probe of human cathepsin L: D. Dana, et al.; Bioorg. Chem.
85, 505 (2019),
Application(s): Activity assay,
Abstract;
Exploring the putative role of kallikrein-6, calpain-1 and cathepsin-D in the proteolytic degradation of α-synuclein in multiple system atrophy: A.P. Kiely, et al.; Neuropathol. Appl. Neurobiol.
45, 347 (2019),
Abstract;
Tasiamide F, a potent inhibitor of cathepsins D and E from a marine cyanobacterium: F.H. Al-Awadhi, et al.; Bioorg. Med. Chem.
24, 3276 (2016),
Application(s): In vitro protease inhibition assays,
Abstract;
Development of a highly potent, selective, and cell-active Inhibitor of cysteine cathepsin L-A hybrid design approach: D. Dana, et al.; Chem. Commun. (Camb.)
50, 10875 (2014),
Abstract;
Development of cell-active non-peptidyl inhibitors of cysteine cathepsins: D. Dana, et al.; Bioorg. Med. Chem.
21, 2975 (2013),
Abstract;
