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Cathepsin substrate
BML-P229-0010 10 mg 243.00 USD
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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)
Sequence:Z-Leu-Arg-AMC . HCl [Z=Cbz=Benzyloxycarbonyl; AMC=7-amino-4-methylcoumarin]
Purity:≥97% (HPLC)
Appearance:White to off-white solid.
Solubility:Soluble in DMSO to at least 20mM.
Shipping:Blue Ice
Long Term Storage:-20°C
Use/Stability:Store, as supplied, at -20°C for up to 1 year. Store solutions at -20°C for up to 3 months.
Handling:Protect from light and moisture.
Regulatory Status:RUO - Research Use Only

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

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