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) |
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Sequence: | Mca-Ala-Pro-Lys(Dnp) [Mca=(7-methoxycoumarin-4-yl)acetyl;Dnp=2,4-dinitrophenyl] |
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Formula: | C32H37N6O12 |
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MW: | 696.7 |
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Source: | Synthetic. |
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Purity: | ≥95% (HPLC) |
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Identity: | Determined by MS. |
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Appearance: | Yellow powder. |
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Solubility: | Soluble in DMSO or 10% Ammonium Hydroxide (2 mg/ml). |
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Shipping: | Blue Ice |
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Long Term Storage: | -20°C |
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Use/Stability: | Stock solutions in DMSO stable at -20°C |
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Handling: | Protect from light and moisture. |
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Regulatory Status: | RUO - Research Use Only |
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Product Literature References
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Exploring Renal Changes after Bariatric Surgery in Patients with Severe Obesity: A. Oliveras, et al.; J. Clin. Med.
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Plasmatic renin-angiotensin system in normotensive and hypertensive patients hospitalized with COVID-19: M.G. Silva, et al.; Biomed. Pharmacother.
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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.
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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
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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.
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Abstract;
Both Specific Endothelial and Proximal Tubular Adam17 Deletion Protect against Diabetic Nephropathy: V. Palau, et al.; Int. J. Mol. Sci.
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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
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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.
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Abstract;
Chymase-dependent production of angiotensin II: an old enzyme in old hearts: G. Froogh, et al.; Am. J. Physiol. Heart Circ. Physiol.
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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