Z-Phe-Arg-AMC | Fluorogenic cathepsin substrate

CAS:
70382-26-2
Catalog Number:
10-5385
Activity:
Fluorogenic cathepsin substrate
Alternate Name:
Z-FR-AMC hydrochloride; Cbz-Phe-Arg-AMC hydrochloride
Molecular Weight:
619.14
Molecular Formula:
C33H36N6O6·HCl
Solubility:
Soluble in DMSO (50 mg/ml)
Physical Properties:
White solid
Purity:
>98% HPLC
Amino acid analysis and identity: Confirmed
Peptide content:
94%
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$45.00
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Z-Phe-Arg-AMC (70382-26-2) is a fluorogenic substrate1 for the following cathepsins (kcat/Km in M-1s-1): B (105)2, C/DPP-I (104)3, F (106)4, K/O2 (105)3, L (106)3, L2/V (105)5, O6, S (104)7, X/Z (104)8. The peptide is also cleaved by plasma kallikrein and kallikrein 89, and papain (kcat/Km=105 M-1s-1).3 Excitation: 365nm, Emission: 440nm.5

References/Citations:

  1. Tavares et al. (2004), Design of potent, selective, and orally bioavailable inhibitors of cysteine protease cathepsin k; J. Med. Chem., 47 588
  2. Therrien et al. (2001), Cathepsins X and B can be differentiated through their respective mono- and dipeptidyl carboxypeptidase activities; Biochemistry, 40 2702
  3. Nägler et al. (1999), Interdependency of sequence and positional specificities for cysteine proteases of the papain family; Biochemistry, 38 4868
  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. Velasco et al. (1994), Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and expression analysis in in human tissues; J. Biol. Chem., 269 27136
  7. Kopitar et al. (1996), Folding and activation of human procathepsin S from inclusion bodies produced in Escherichia coli; Eur. J. Biochem., 236 558
  8. Klemenčič et al. (2000), Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase; Eur. J. Biochem., 267 5404
  9. Kishi et al. (2006), Activation and enzymatic characterization of recombinant human kallikrein 8; Biol. Chem., 387 723
CAS:
70382-26-2
Catalog Number:
10-5385
Activity:
Fluorogenic cathepsin substrate
Alternate Name:
Z-FR-AMC hydrochloride; Cbz-Phe-Arg-AMC hydrochloride
Molecular Weight:
619.14
Molecular Formula:
C33H36N6O6·HCl
Solubility:
Soluble in DMSO (50 mg/ml)
Physical Properties:
White solid
Purity:
>98% HPLC
Amino acid analysis and identity: Confirmed
Peptide content:
94%
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-Phe-Arg-AMC (70382-26-2) is a fluorogenic substrate1 for the following cathepsins (kcat/Km in M-1s-1): B (105)2, C/DPP-I (104)3, F (106)4, K/O2 (105)3, L (106)3, L2/V (105)5, O6, S (104)7, X/Z (104)8. The peptide is also cleaved by plasma kallikrein and kallikrein 89, and papain (kcat/Km=105 M-1s-1).3 Excitation: 365nm, Emission: 440nm.5

References/Citations:

  1. Tavares et al. (2004), Design of potent, selective, and orally bioavailable inhibitors of cysteine protease cathepsin k; J. Med. Chem., 47 588
  2. Therrien et al. (2001), Cathepsins X and B can be differentiated through their respective mono- and dipeptidyl carboxypeptidase activities; Biochemistry, 40 2702
  3. Nägler et al. (1999), Interdependency of sequence and positional specificities for cysteine proteases of the papain family; Biochemistry, 38 4868
  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. Velasco et al. (1994), Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and expression analysis in in human tissues; J. Biol. Chem., 269 27136
  7. Kopitar et al. (1996), Folding and activation of human procathepsin S from inclusion bodies produced in Escherichia coli; Eur. J. Biochem., 236 558
  8. Klemenčič et al. (2000), Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase; Eur. J. Biochem., 267 5404
  9. Kishi et al. (2006), Activation and enzymatic characterization of recombinant human kallikrein 8; Biol. Chem., 387 723

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

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

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