Human ACE/CD143 Antibody Summary
Leu30-Leu1261
Accession # P12821
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Detection of ACE/CD143 in Human Mature Monocyte-derived Dendritic Cells by Flow Cytometry. Human mature monocyte-derived dendritic cells were stained with Goat Anti-Human ACE/CD143 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF929, filled histogram) or isotype control antibody (Catalog # AB-108-C, open histogram), followed by Allophycocyanin-conjugated Anti-Goat IgG Secondary Antibody (Catalog # F0108).
ACE/CD143 in Human Kidney. ACE/CD143 was detected in immersion fixed paraffin-embedded sections of human kidney using 15 µg/mL Goat Anti-Human ACE/CD143 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF929) overnight at 4 °C. Tissue was stained with the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
ACE/CD143 in Human Kidney. ACE/CD143 was detected in immersion fixed paraffin-embedded sections of human kidney array using Goat Anti-Human ACE/CD143 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF929) at 15 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Lower panel shows a lack of labeling if primary antibodies are omitted and tissue is stained only with secondary antibody followed by incubation with detection reagents. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
Detection of Human ACE/CD143 by Immunocytochemistry/ Immunofluorescence Overview of Multi-dimensional Microscopic Molecular Profiling (MMMP).The overall MMMP approach is depicted using an example tissue section from normal human duodenum (sample #1.9.7). (a) Slides were subjected to repeated cycles of staining and imaging with fluorescent primary antibodies and DAPI. At the end of each cycle, fluorescent signal was removed by a chemical bleaching process, and slides were again imaged, before proceeding to the next round of this iterative procedure. After the final antibody stain (#15 Sma), slides were analyzed with a series of histochemical stains. (b) A set of tiling images spanning each tissue section was initially generated by the microscope system. The tiling images were then computationally ‘stitched’ together to produce a single image per staining cycle for each sample. (c) Image registration was performed to align images from the same tissue section across cycles. Mean intensities of the DAPI signal from all immuno-fluorescence images are shown from before (Unregistered) and after (Registered) the image registration procedure was completed. (d) Following registration, signal intensities from the relevant channels for each image (columns) in the MMMP series were extracted for each pixel (rows) within the tissue section and compiled into a large data matrix of in situ molecular profiles. Image collected and cropped by CiteAb from the following open publication (https://dx.plos.org/10.1371/journal.pone.0128975), licensed under a CC-BY license. Not internally tested by R&D Systems.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: ACE/CD143
ACE (also known as peptidyl-dipetidase A) is a zinc metallopeptidase important for blood pressure control and water and salt metabolism (2). It cleaves the C-terminal dipeptide from angiotensin I to produce the potent vasopressor octapeptide angiotensin II and inactivates bradykinin by the sequential removal of two C-terminal dipeptides. In addition to the two physiological substrates, ACE cleaves C-terminal dipeptides from various oligopeptides with a free C-terminus. Because of its location and specificity, ACE plays additional roles in immunity, reproduction and neuropeptide regulation. For example, ACE degrades Alzheimer amyloid beta -peptide (A beta ), retards A beta aggregation, deposition, fibril formation, and inhibits cytotoxicity (3).
ACE is a type I membrane protein and exists in two isoforms (2). Somatic ACE, found in endothelial, epithelial and neuronal cells, comprises two highly similar domains called N- and C-domains, each of which contains the HExxH consensus sequence for zinc binding. Germinal ACE, found exclusively in the testes, comprises a single catalytically active domain identical to the C-domain of somatic ACE except for an N-terminal 67 residue germinal ACE-specific sequence. Physiological functions of the two tissue-specific isozymes are not interchangeable (4). For example, sperm-specific expression of the germinal ACE, not the somatic ACE, in ACE knockout male mice restored fertility.
Soluble ACE is present in many biological fluids, such as serum, seminal fluid, amniotic fluid and cerebrospinal fluid (2). The soluble ACE is derived from the membrane forms by actions of secretases or sheddases. The identities of the secretases have not been revealed, although they belong to the family of zinc metallopeptidases (5, 6).
- Soubrier, et al. (1988) Proc. Natl. Acad. Sci. USA 85:9386.
- Corvol, P. and T.A. Williams (1998) in Handbook of Proteolytic Enzymes. Barrett, A.J. et al. (eds): San Diego, Academic Press, p. 1066.
- Hu, et al. (2001) J. Biol. Chem. 276:47863.
- Kessler, et al. (2000) J. Biol. Chem. 275:26259.
- Eyries, et al. (2001) J. Biol. Chem. 276:5525.
- Alfalah, et al. (2001) J. Biol. Chem. 276:21105.
Product Datasheets
Citations for Human ACE/CD143 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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miR-6869-5p Transported by Plasma Extracellular Vesicles Mediates Renal Tubule Injury and Renin-Angiotensin System Activation in Obesity
Authors: Liu HH, Li XQ, Liu JF et al.
Frontiers in Medicine
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Distinctive Properties of Endothelial Cells from Tumor and Normal Tissue in Human Breast Cancer
Authors: K Wilkus, K Brodaczews, A Kajdasz, C Kieda
International Journal of Molecular Sciences, 2021-08-17;22(16):.
Species: Human
Sample Types: Whole Cells
Applications: Flow Cytometry -
Automated Analysis and Classification of Histological Tissue Features by Multi-Dimensional Microscopic Molecular Profiling.
Authors: Riordan D, Varma S, West R, Brown P
PLoS ONE, 2015-07-15;10(7):e0128975.
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New perspectives in the renin-angiotensin-aldosterone system (RAAS) II: albumin suppresses angiotensin converting enzyme (ACE) activity in human.
Authors: Fagyas M, Uri K, Siket I, Fulop G, Csato V, Darago A, Boczan J, Banyai E, Szentkiralyi I, Maros T, Szerafin T, Edes I, Papp Z, Toth A
PLoS ONE, 2014-04-01;9(4):e87844.
Species: Human
Sample Types: Serum
Applications: Western Blot -
Synthetic reconstruction of zoonotic and early human severe acute respiratory syndrome coronavirus isolates that produce fatal disease in aged mice.
Authors: Rockx B, Sheahan T, Donaldson E, Harkema J, Sims A, Heise M, Pickles R, Cameron M, Kelvin D, Baric R
J. Virol., 2007-05-16;81(14):7410-23.
Species: Primate - Chlorocebus pygerythrus (Vervet Monkey)
Sample Types: Whole Cells
Applications: Neutralization
FAQs
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Is ACE-1 the same as ACE?
Yes. ACE-1 is used as an alternative name, but not as commonly as ACE and CD143.
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