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Mca-APK(Dnp)

ACE substrate
 
BML-P163-0001 1 mg 121.00 USD
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Fluorogenic substrate for angiotensin converting enzyme-2 (ACE2), a zinc-dependent carboxypeptidase with 42% amino acid sequence identity to ACE1. Unlike Mca-YVADAPK(Dnp), this substrate is not cleaved by caspases. Mca fluorescence is quenched by the Dnp group until cleavage (at Pro-Lys) separates them. Ex: 328 nm, Em: 393 nm, although the following Ex/Em have also been used: 320-340/400-420. This highly quenched (99.6%) substrate is useful for inhibitor screening and kinetic analysis. Also available: fluorogenic Mca control peptide (BML-P127).

Product Specification

Alternative Name:ACE2 substrate (fluorogenic)
 
Sequence:Mca-Ala-Pro-Lys(Dnp)-OH  [Mca=(7-methoxycoumarin-4-yl)acetyl;Dnp=2,4-dinitrophenyl]
 
Formula:C32H37N6O12
 
MW:697.7
 
Source:Synthetic.
 
Purity:≥95% (HPLC)
 
Appearance:Yellow powder.
 
Solubility:Soluble in DMSO or 10% Ammonium Hydroxide (2 mg/ml).
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:-20°C
 
Use/Stability:Stock solutions in DMSO stable at -20°C
 
Handling:Protect from light and moisture.
 

Product Literature References

Chymase-dependent production of angiotensin II: an old enzyme in old hearts: G. Froogh, et al.; Am. J. Physiol. Heart Circ. Physiol. 312, H223 (2017), Abstract;
Estradiol, acting through ERα, induces endothelial non-classic renin-angiotensin system increasing angiotensin 1-7 production: A. Mompeon, et al. ; Mol. Cell. Endocrinol. 422, 1 (2016), Abstract;
Urinary Angiotensin Converting Enzyme 2 Increases in Patients With Type 2 Diabetic Mellitus: Y. Liang, et al.; Kidney Blood Press. Res. 40, 101 (2015), Application(s): Fluorescent Substrate-Based Assay, Abstract; Full Text
Angiotensin-converting enzyme-2 (ACE2): comparative modeling of the active site, specificity requirements, and chloride dependence: J.L. Guy, et al.; Biochemistry 42, 13185 (2003), Abstract;
ACEH/ACE2 is a novel mammalian metallocarboxypeptidase and a homologue of angiotensin-converting enzyme insensitive to ACE inhibitors: A.J. Turner, et al.; Can. J. Physiol. Pharmacol. 80, 346 (2002), Abstract;
Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase: C. Vickers, et al.; J. Biol. Chem. 277, 14838 (2002), Abstract; Full Text
A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9: M. Donoghue, et al.; Circ. Res. 87, E1 (2000), Abstract; Full Text

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Angiotensin converting enzyme
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