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Mca-APK(Dnp)

ACE2 substrate
 
BML-P163-0001 1 mg 143.00 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 Details

Alternative Name:ACE2 substrate (fluorogenic)
 
Sequence:Mca-Ala-Pro-Lys(Dnp)  [Mca=(7-methoxycoumarin-4-yl)acetyl;Dnp=2,4-dinitrophenyl]
 
Formula:C32H37N6O12
 
MW:696.7
 
Source:Synthetic.
 
Purity:≥95% (HPLC)
 
Identity:Determined by MS. 
 
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.
 
Regulatory Status:RUO - Research Use Only
 

Product Literature References

Exploring Renal Changes after Bariatric Surgery in Patients with Severe Obesity: A. Oliveras, et al.; J. Clin. Med. 11, 728 (2022), Abstract;
Plasmatic renin-angiotensin system in normotensive and hypertensive patients hospitalized with COVID-19: M.G. Silva, et al.; Biomed. Pharmacother. 152, 113201 (2022), Abstract;
A pilot study to assess the circulating renin-angiotensin system in COVID-19 acute respiratory failure: D.C. Files, et al.; Am. J. Physiol. Lung Cell. Mol. Physiol. 321, L213 (2021), Abstract;
A Pilot Study to Assess the Circulating Renin-Angiotensin-System in COVID-19 Acute Respiratory Failure: D.C. Files, et al.; Am. J. Physiol. Lung Cell. Mol. Physiol. (2021), Abstract;
Activation of angiotensin-converting enzyme 2/angiotensin (1–7)/mas receptor axis triggers autophagy and suppresses microglia proinflammatory polarization via forkhead box class O1 signaling: R. Dang, et al.; Aging Cell 20, 13480 (2021), Abstract;
Apelin-13 in septic shock: effective in supporting hemodynamics in sheep but compromised by enzymatic breakdown in patients: D. Coquerel, et al.; Sci. Rep. 11, 22770 (2021), Abstract;
Both Specific Endothelial and Proximal Tubular Adam17 Deletion Protect against Diabetic Nephropathy: V. Palau, et al.; Int. J. Mol. Sci. 22, 5520 (2021), Abstract;
Male bias in ACE2 basic science research: Missed opportunity for discovery in the time of COVID-19: B. Stanic., et al.; Am. J. Physiol. Regul. Integr. Comp. Physiol. 1152, 356 (2021), Abstract;
Metabolism of angiotensin peptides by angiotensin converting enzyme 2 (ACE2) and analysis of the effect of excess zinc on ACE2 enzymatic activity: Y. Polak & R.C. Speth; Peptides 137, 170477 (2021), Abstract;
SARS-CoV-2 Infection Modulates ACE2 Function and Subsequent Inflammatory Responses in Swabs and Plasma of COVID-19 Patients: L. Gutiérrez-Chamorro, et al.; Viruses 13, 1715 (2021), Abstract;
Role of the Renin Angiotensin System in Blood Pressure Allostasis-induced by Severe Food Restriction in Female Fischer rats: A.M.A. de Souza, et al.; Sci. Rep. 8, 10327 (2018), Abstract;
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;
Serum activity of angiotensin converting enzyme 2 is decreased in patients with acute ischemic stroke: D.M. Bennion, et al.; J. Renin Angiotensin Aldosterone Syst. 17, 1470320316661060 (2016), Abstract; Full Text
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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