Anti-Angiotensin Converting Enzyme 1 antibody [EPR22291-89] - BSA and Azide free (Capture)

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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 : 15615692, PubMed : 20826823, PubMed : 2558109, PubMed : 4322742, PubMed : 7523412, PubMed : 7683654). Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates (PubMed : 10913258, PubMed : 1320019, PubMed : 1851160, PubMed : 19773553, PubMed : 7683654, PubMed : 7876104). 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 : 11432860, PubMed : 1851160, PubMed : 19773553, PubMed : 23056909, PubMed : 4322742). Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response (PubMed : 15615692, PubMed : 2558109, PubMed : 4322742, PubMed : 6055465, PubMed : 6270633, PubMed : 7683654). Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins (PubMed : 15615692, PubMed : 6208535, PubMed : 6270633, PubMed : 656131). Catalyzes degradation of different enkephalin neuropeptides (Met-enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met-enkephalin-Arg-Gly-Leu) (PubMed : 2982830, PubMed : 6270633, PubMed : 656131). 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 : 26403559, PubMed : 7876104, PubMed : 8257427, PubMed : 8609242). 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 : 10336644, PubMed : 2983326, PubMed : 7683654, PubMed : 9371719). 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 : 10336644, PubMed : 19773553, PubMed : 7876104).. Angiotensin-converting enzyme, soluble form. Soluble form that is released in blood plasma and other body fluids following proteolytic cleavage in the juxtamembrane stalk region.. Isoform Testis-specific. Isoform produced by alternative promoter usage that is specifically expressed in spermatocytes and adult testis, and which is required for male fertility (PubMed : 1651327, PubMed : 1668266). In contrast to somatic isoforms, only contains one catalytic domain (PubMed : 1651327, PubMed : 1668266). Acts as a dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of substrates (PubMed : 1668266, PubMed : 24297181). The identity of substrates that are needed for male fertility is unknown (By similarity). May also have a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. The GPIase activity was reported to be essential for the egg-binding ability of the sperm (By similarity). This activity is however unclear and has been challenged by other groups, suggesting that it may be indirect (By similarity).