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Procathepsin V (human), (recombinant) (His-tag)

 
BML-SE554-0010 10 µg 457.00 USD
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Full-length proenzyme. Can be activated in one step.

Product Specification

Alternative Name:Cathepsin L2
 
MW:~37kDa (SDS-PAGE)
 
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.
 
EC:3.4.22.38
 
UniProt ID:O60911
 
Formulation:Liquid. In 25mM TRIS-HCl, pH 8.0, containing 100mM sodium chloride, 0.05% Tween-20 and 10% glycerol.
 
Purity:≥90%
 
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.
 
Application Notes:Useful tool to study enzyme kinetics, cleave target substrates and screen for inhibitors.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Use/Stability:Avoid extended periods unfrozen. This enzyme is stable for 6 months when stored as received under the above conditions.
 
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
 
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.
 
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.
 

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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BML-P229-0010 10 mg 180.00 USD
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