Full-length proenzyme. Can be activated in one step.
Product Details
Alternative Name: | Cathepsin L2 |
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MW: | ~37kDa (SDS-PAGE) |
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Source: | Produced in insect cells. Recombinant glycosylated procathepsin V cloned from human cDNA and purified as full-length proenzyme. Produced in a baculovirus expression system. |
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EC: | 3.4.22.38 |
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UniProt ID: | O60911 |
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Formulation: | Liquid. In 25mM TRIS-HCl, pH 8.0, containing 100mM sodium chloride, 0.05% Tween-20 and 10% glycerol. |
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Purity: | ≥90% |
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Specific Activity: | 436 U/µg protein. One unit will hydrolyze one pmole Z-Leu-Arg-AMC substrate (Prod. No. BML-P229, 25 µM) per minute at 25°C, in 25mM NaOAc pH 5.5, 100mM NaCl, 1.0mM DTT. |
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Application Notes: | Useful tool to study enzyme kinetics, cleave target substrates and screen for inhibitors. |
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Shipping: | Dry Ice |
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Long Term Storage: | -80°C |
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Use/Stability: | Avoid extended periods unfrozen. This enzyme is stable for 6 months when stored as received under the above conditions. |
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Handling: | Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C. |
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Scientific Background: | Cathepsin V, a member of the papain family of cysteine proteases, has 78% identity to cathepsin L, but unlike cathepsin L is not widely expressed, being localized to thymus, testis, corneal epithelium, and macrophages. It is a strong elastase, also cleaving proteins such as the invariant chain (Ii), plasminogen, and kininogen. It is implicated in disease states such as cancer, angiogenesis, atherosclerosis, and myasthenia gravis. |
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Technical Info/Product Notes: | The proenzyme can be activated as in Adachi et al. (Reference year 2008): Dilute proenzyme into 200mM NaAcetate, pH 6.0, with 0.05% SDS, 2.5mM DTT, and incubate at 37°C for 5-30 minutes. Alternatively, pre-incubate proenzyme 5-30 minutes in assay buffer (25mM NaOAc pH 5.5, 100mM sodium chloride, 1.0mM DTT), then add substrate to begin assay. Incubation times must be determined empirically; activation is dependent on factors such as buffer, temperature, and enzyme concentration, and cathepsin V will autodegrade once activated. |
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Regulatory Status: | RUO - Research Use Only |
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General Literature References
Cathepsin V, but not cathepsins L, B and K, may release angiostatin-like fragments from plasminogen: L. Puzer, et al.; Biol. Chem.
389, 195 (2008),
Abstract;
DNA accelerates the inhibition of human cathepsin V by serpins: P.C. Ong, et al.; J. Biol. Chem.
282, 36980 (2007),
Abstract;
Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages: Y. Yasuda, et al.; J. Biol. Chem.
279, 36761 (2004),
Abstract;
Comparative substrate specificity analysis of recombinant human cathepsin V and cathepsin L: L. Puzer, et al.; Arch. Biochem. Biophys.
430, 274 (2004),
Abstract;
Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis: E. Tolosa, et al.; J. Clin. Invest.
112, 517 (2003),
Abstract;
Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas: I. Santamaria, et al.; Cancer Res.
58, 1624 (1998),
Abstract;
Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium: W. Adachi, et al.; Invest. Ophthalmol. Vis. Sci.
39, 1789 (1998),
Abstract;
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