Human ACE/CD143 Biotinylated Antibody

Catalog # Availability Size / Price Qty
BAF929
ACE/CD143 in Human Kidney.
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Citations (1)
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Human ACE/CD143 Biotinylated Antibody Summary

Species Reactivity
Human
Specificity
Detects human ACE/CD143 in Western blots. In Western blots, less than 1% cross-reactivity with recombinant human ACE‑2 is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant human ACE/CD143
Leu30-Leu1261
Accession # P12821.1
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Label
Biotin

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Human ACE/CD143 Somatic Form (Catalog # 929-ZN)
Immunohistochemistry
5-15 µg/mL
See below

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

Immunohistochemistry ACE/CD143 antibody in Human Kidney by Immunohistochemistry (IHC-P). View Larger

ACE/CD143 in Human Kidney. ACE/CD143 was detected in immersion fixed paraffin-embedded sections of human kidney using Goat Anti-Human ACE/CD143 Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF929) 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). View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.

Reconstitution Calculator

Reconstitution Calculator

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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Shipping
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 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).

References
  1. Soubrier, et al. (1988) Proc. Natl. Acad. Sci. USA 85:9386.
  2. Corvol, P. and T.A. Williams (1998) in Handbook of Proteolytic Enzymes. Barrett, A.J. et al. (eds): San Diego, Academic Press, p. 1066.
  3. Hu, et al. (2001) J. Biol. Chem. 276:47863.
  4. Kessler, et al. (2000) J. Biol. Chem. 275:26259.
  5. Eyries, et al. (2001) J. Biol. Chem. 276:5525.
  6. Alfalah, et al. (2001) J. Biol. Chem. 276:21105.
Long Name
Angiotensin I Converting Enzyme
Entrez Gene IDs
1636 (Human); 11421 (Mouse)
Alternate Names
ACE; ACE1angiotensin converting enzyme, somatic isoform; angiotensin I converting enzyme (peptidyl-dipeptidase A) 1; carboxycathepsin; CD143 antigen; CD143; DCP; DCP1; DCP1angiotensin-converting enzyme; dipeptidyl carboxypeptidase 1; Dipeptidyl carboxypeptidase I; EC 3.2.1.-; EC 3.4.15.1; Kininase II; MGC26566; MVCD3; peptidase P; testicular ECA

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Citation for Human ACE/CD143 Biotinylated 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.

1 Citation: Showing 1 - 1

  1. 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: Immunoprecipitation

FAQs

  1. 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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