Sensitive fluorogenic substrate for cathepsin K (Km=8µM, kcat/Km=4 x 10 M-1s-1). This substrate is also cleaved by cathepsin B, F, L, L2/V, S. Z-LR-AMC is also cleaved by malaria parasite cysteine proteases falcipain-1, -2, -3, berghepain, and vivapain-2, -3. Ex.: 365nm, Em.: 440nm, although the following Ex/Em can also be used: 355,380/450,460. This substrate is useful for inhibitor screening and kinetic analysis. Also available: fluorogenic calibration standard AMC (BML-KI144).
Product Details
| Alternative Name: | Z-Leu-Arg-AMC, Cathepsin K substrate (fluorogenic) |
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| Sequence: | Z-Leu-Arg-AMC . HCl [Z=Cbz=Benzyloxycarbonyl; AMC=7-amino-4-methylcoumarin] |
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| MW: | 578.7 |
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| Source: | Synthetic. |
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| Formulation: | Lyophilized. |
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| Purity: | ≥97% (HPLC) |
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| Appearance: | White to off-white solid. |
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| Solubility: | Soluble in DMSO to at least 20mM. |
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| Shipping: | Blue Ice |
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| Long Term Storage: | -20°C |
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| Use/Stability: | Store, as supplied, at -20°C for up to 1 year. Store solutions at -20°C for up to 3 months. |
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| Handling: | Protect from light and moisture. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Impact of Sr2+ and hypoxia on 3D triple cultures of primary human osteoblasts, osteocytes and osteoclasts: K. Wirsig, et al.; Eur. J. Cell Biol.
101, 151256 (2022),
Abstract;
A Clinical-Stage Cysteine Protease Inhibitor blocks SARS-CoV-2 Infection of Human and Monkey Cells: D.M. Mellott, et al.; ACS Chem. Biol.
16, 642 (2021),
Abstract;
Full Text
Fluoride does not inhibit enamel protease activity: C.E. Tye, et al.; J. Dent. Res.
90, 489 (2011),
Application(s): Use of Z-LR-AMC to measure cathepsin K activity,
Abstract;
Full Text
Designed inhibitors of insulin-degrading enzyme regulate the catabolism and activity of insulin: M.A. Leissring, et al.; PLoS One
5, e10504 (2010),
Application(s): Use of Z-LR-AMC to measure cathepsin B activity,
Abstract;
Full Text
A chimeric cysteine protease of Plasmodium berghei engineered to resemble the Plasmodium falciparum protease falcipain-2: A. Singh, et al.; PEDS
20, 171 (2007),
Abstract;
Full Text
Cysteine protease falcipain 1 in Plasmodium falciparum is biochemically distinct from its isozymes: S.L. Goh, et al.; Parasitol. Res.
97, 295 (2005),
Abstract;
Identification and biochemical characterization of vivapains, cysteine proteases of the malaria parasite Plasmodium vivax: B.-K. Na, et al.; Biochem. J.
378, 529 (2004),
Abstract;
Full Text
Independent intramolecular mediators of folding, activity, and inhibition for the Plasmodium falciparum cysteine protease falcipain-2: K.C. Pandey, et al.; J. Biol. Chem.
279, 3484 (2004),
Abstract;
Full Text
Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization: D. Brömme, et al.; Biochemistry
38, 2377 (1999),
Abstract;
Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization: B. Wang, et al.; J. Biol. Chem.
273, 32000 (1998),
Abstract;
Full Text
Expression of human cathepsin K in Pichia pastoris and preliminary crystallographic studies of an inhibitor complex: C.J. Linnevers, et al.; Protein Sci.
6, 919 (1997),
Abstract;
Full Text
Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme: D. Brömme, et al.; J. Biol. Chem.
271, 2126 (1996),
Abstract;
Full Text
Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification: M. Bossard, et al.; J. Biol. Chem.
271, 12517 (1996),
Abstract;
Full Text
