Control peptide for A2295-01N (affinity purified antibody). Synthetic peptide consisting of 14aa peptide of Human testicular-ACE. Species Sequence Homology: Human: 100%; mouse: 92%; rat t-ACE: 57%.||Renin-Angiotensin System (RAS) is a crtical regulator of blood pressure homeostasis. The protease renin cleaves angiotensinogen into inactive decameric peptide angiotensin-I (Ang-I). Angiotensin-converting enzyme (ACE) then cleaves C-terminal dipeptide from Ang-I to form an active octamer angiotensin-II (Ang-II), which can contribute to hypertension by promoting vascular smooth muscle vasocontriction and renal tubule sodium reabsorption. ACE can also cleave many other small peptides including the vasodialating peptide bradykinin into inactive fragment, cleave Alzheimer amyloid beta-peptide (Abeta), retard Abeta aggregation, deposition and fibril formation. ACE mutant mice display spontaneous hypotension, partial male infertility and kidney malformations. ACE is found in somatic (s-ACE) and testicular/germinal (t-ACE) isoforms. The products of renin and ACE catalysis, namely Ang1-10 and Ang1-8 can also be by another peptidase, ACE-2 to Ang1-9 and Ang1-7, respectively. ACE-2 and ACE (s-ACE and t-ACE) are made as transmembrane (TM) proteins but these enzymes also exist as soluble, truncated forms lacking the TM and cytosolic domains.||ACE (also known as dipeptidyl carboxypeptidase-1, DCP1; Kininase-II, ACE1) gene has been mapped at human chromosome 17q23. The s-ACE and t-ACE isoforms are generated by alternative splicing of ACE-2 gene. Somatic-ACE, a Zn (II) containing dipeptidyl carboxy peptidase is a single chain glycoprotein with a molecular mass of ~140kDa. The s-ACE enzymes from mouse (1312aa), rat (1313aa) and human (1306aa) contain two large areas of homologous sequence, each containing catalytic site and a Zn-binding region. These homologous regions are approximately half the size of whole s-ACE. The s-ACE is expressed in many somatic tissue tissues, including vascular endothelial cells, renal epithelial cells, and testicular Leydig cells. In contrast to s-ACE, the t-ACE enzymes (~80kD) from mouse (732aa), rat (775aa) and human (732aa) contain only one active site and are expressed only in sperms. The soluble ACE is present present in serum and seminal, amniotic and cerebrospinal fluids. The t-ACE is identical, from residue 37 to its C-terminus, to the second half or C-terminus of s-ACE. The t-ACE from mouse, rat and human are ~72% identical to each other in their aa seq.

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