Human Angiotensin I Converting Enzyme (ACE) ELISA Kit

Due to the possibility of mismatching between antigens from other origin and antibodies used in our kits (e.g., antibody targets conformational epitope rather than linear epitope), some native or recombinant proteins from other manufacturers may not be recognized by our products.

Principle of the Assay

The microtiter plate provided in this kit has been pre-coated with an antibody specific to ACE. Standards or samples are then added to the appropriate microtiter plate wells with a biotin-conjugated antibody preparation specific to ACE. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After the TMB substrate solution is added, only those wells that contain ACE, biotin-conjugated antibody, and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution, and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of ACE in the samples is then determined by comparing the O.D. of the samples to the standard curve.


For Use with serum, plasma, and cell culture supernatants. For Research Use Only. Not for use in diagnostic procedures.

Target Information

Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity (PubMed:2558109, PubMed:4322742, PubMed:7683654, PubMed:7523412, PubMed:15615692, PubMed:20826823). Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates (PubMed:1851160, PubMed:1320019, PubMed:7683654, PubMed:7876104, PubMed:10913258, PubMed:19773553). Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin (PubMed:4322742, PubMed:1851160, PubMed:11432860, PubMed:19773553, PubMed:23056909). Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response (PubMed:2558109, PubMed:6055465, PubMed:4322742, PubMed:6270633, PubMed:7683654, PubMed:15615692). Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins (PubMed:656131, PubMed:6270633, PubMed:6208535, PubMed:15615692). Catalyzes degradation of different enkephalin neuropeptides (Met-enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met-enkephalin-Arg-Gly-Leu) (PubMed:656131, PubMed:6270633, PubMed:2982830). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin (By similarity). Met-enkephalin-Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long-term synaptic potentiation of glutamate release (By similarity). Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) (PubMed:8257427, PubMed:7876104, PubMed:8609242, PubMed:26403559). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (PubMed:18077343). Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation (PubMed:11604391, PubMed:16154999, PubMed:19773553). Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones (PubMed:2983326, PubMed:7683654, PubMed:9371719, PubMed:10336644). Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region (PubMed:7876104, PubMed:10336644, PubMed:19773553).

Materials Supplied

Storage

Performance Characteristics