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



BML-SE554-0010	10 µg	602.00 USD
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Full-length proenzyme. Can be activated in one step.

Product Details

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:	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.

Regulatory Status:	RUO - Research Use Only

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;