Z-Leu-Arg-AMC | Fluorogenic Cathepsin K substrate

CAS:
156192-32-4
Catalog Number:
10-5386
Activity:
Fluorogenic cathepsin substrate
Alternate Name:
Z-LR-AMC hydrochloride; Cbz-Leu-Arg-AMC hydrochloride
Molecular Weight:
615.13
Molecular Formula:
C30H38N6O6·HCl
Solubility:
Soluble in DMSO (20 mg/ml)
Physical Properties:
White solid
Purity:
>97% HPLC
Amino acid analysis and identity: Confirmed
Peptide content:
93%
Storage Temperature:
-20°C
Stability:
Stable for 2 years from date of purchase as supplied. Solutions in DMSO may be stored at -20°C for up to 3 months. Protect from light!
Shipping Code:
RT

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5 mg$80.00
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Z-Leu-Arg-AMC (156192-32-4) is a sensitive Cathepsin K fluorogenic substrate (Km=8µM, kcat/Km=4 x 105 M-1s-1)1-3. It is cleaved more slowly by the following cathepsins (kcat/Km: B (105)4, F (106)4, L (106)4,5, L2/V (104)5, S (105)2,4,5. Also cleaved by malaria parasite proteases berghepain6, vivapain-2 and -37, and falcipain-1, -2, and -36,8,9. Excitation: 365nm, Emission: 440nm.

References/Citations:

  1. Bossard et al. (1996), Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification; J. Biol. Chem. 271 12517
  2. Brömme et al. (1996), 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; J. Biol. Chem. 271 2126
  3. Linnevers et al. (1997), Expression of human cathepsin K in Pichia pastoris and preliminary crystallographic studies of an inhibitor complex; Protein Sci. 6 919
  4. Wang et al. (1998), Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization; J. Biol. Chem., 273 32000
  5. Brömme et al. (1999), Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization and chromosomal localization; Biochemistry, 38 2377
  6. Singh et al. (2007), A chimeric cysteine protease of Plasmodium berghei engineered to resemble the Plasmodium falciparum protease falcipain-2; Protein Eng. Des. Sel. 20 171
  7. Na et al. (2004), Identification and biochemical characterization of vivapains, cysteine proteases of the malaria parasite Plasmodium vivax; Biochem. J. 378(Pt2) 529
  8. Goh et al. (2005), Cysteine protease falcipain 1 in Plasmodium falciparum is biochemically distinct from its isozymes; Parasitol. Res. 97 295
  9. Pandey et al. (2004), Independent intramolecular mediators of folding, activity, and inhibition for the Plasmodium falciparum cysteine protease falcipain-2; J. Biol. Chem. 279 3484
CAS:
156192-32-4
Catalog Number:
10-5386
Activity:
Fluorogenic cathepsin substrate
Alternate Name:
Z-LR-AMC hydrochloride; Cbz-Leu-Arg-AMC hydrochloride
Molecular Weight:
615.13
Molecular Formula:
C30H38N6O6·HCl
Solubility:
Soluble in DMSO (20 mg/ml)
Physical Properties:
White solid
Purity:
>97% HPLC
Amino acid analysis and identity: Confirmed
Peptide content:
93%
Storage Temperature:
-20°C
Stability:
Stable for 2 years from date of purchase as supplied. Solutions in DMSO may be stored at -20°C for up to 3 months. Protect from light!
Shipping Code:
RT

Safety Data Sheet:

N/A

Product Data Sheet:

Download Product Data Sheet

Materials provided by Focus Biomolecules are for laboratory research use only and are not intended for human or veterinary applications. Please note that we do not sell to individuals and that all orders placed by non-research organizations will incur a $20 restocking/refund fee

Z-Leu-Arg-AMC (156192-32-4) is a sensitive Cathepsin K fluorogenic substrate (Km=8µM, kcat/Km=4 x 105 M-1s-1)1-3. It is cleaved more slowly by the following cathepsins (kcat/Km: B (105)4, F (106)4, L (106)4,5, L2/V (104)5, S (105)2,4,5. Also cleaved by malaria parasite proteases berghepain6, vivapain-2 and -37, and falcipain-1, -2, and -36,8,9. Excitation: 365nm, Emission: 440nm.

References/Citations:

  1. Bossard et al. (1996), Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification; J. Biol. Chem. 271 12517
  2. Brömme et al. (1996), 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; J. Biol. Chem. 271 2126
  3. Linnevers et al. (1997), Expression of human cathepsin K in Pichia pastoris and preliminary crystallographic studies of an inhibitor complex; Protein Sci. 6 919
  4. Wang et al. (1998), Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization; J. Biol. Chem., 273 32000
  5. Brömme et al. (1999), Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization and chromosomal localization; Biochemistry, 38 2377
  6. Singh et al. (2007), A chimeric cysteine protease of Plasmodium berghei engineered to resemble the Plasmodium falciparum protease falcipain-2; Protein Eng. Des. Sel. 20 171
  7. Na et al. (2004), Identification and biochemical characterization of vivapains, cysteine proteases of the malaria parasite Plasmodium vivax; Biochem. J. 378(Pt2) 529
  8. Goh et al. (2005), Cysteine protease falcipain 1 in Plasmodium falciparum is biochemically distinct from its isozymes; Parasitol. Res. 97 295
  9. Pandey et al. (2004), Independent intramolecular mediators of folding, activity, and inhibition for the Plasmodium falciparum cysteine protease falcipain-2; J. Biol. Chem. 279 3484

Focus Biomolecules • Plymouth Meeting, PA USA • 1-855-FOCUS21

Focus Biomolecules
Plymouth Meeting, PA USA
1-855-FOCUS21

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