ACE Antibody (YA5105)
(Synonyms: ACE; DCP; DCP1; Angiotensin-converting enzyme; ACE; Dipeptidyl carboxypeptidase I; Kininase II; CD antigen CD143)ACE Antibody (YA5105) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to ACE.
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Host:
Mouse
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Application:
WB
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Reactivity :
Human, Mouse, Rat, Bovine
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Formulation:
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
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Conjugation:
Non-conjugated
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Applications
| Application |
WB
WB: Western Blot
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|---|---|
| Dilution Ratio | 1:1000-1:2000 |
Product Details
ACE Antibody (YA5105) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to ACE.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat, Bovine
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Calculated Molecular Weight Predicted band size: 150 kDa;
Purified recombinant human ACE1 (N-terminus) protein fragments expressed in E.coli.
affinity purified.
Non-conjugated
Unmodified
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Versand
Shipping with blue ice.
Background
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Function
ACE is a two-domain dipeptidylcarboxypeptidase that regulates blood pressure through the renin-angiotensin-aldosterone system and kallikrein-kinin system[1]. Mechanistically, ACE converts Ang I to Ang II and degrades bradykinin, linking vasoconstrictor generation with vasodilator peptide inactivation[1][2]. In vivo, the C-domain is the predominant site for Ang I cleavage, whereas both ACE domains can hydrolyze bradykinin[3][1]. Compared with ACE2, ACE functions as a dipeptidylcarboxypeptidase, while ACE2 is a carboxypeptidase that metabolizes angiotensin peptides and is not inhibited by typical ACE inhibitors[4][5]. Therefore, ACE and ACE2 define distinct but connected enzymatic axes for cardiovascular, renal, and inflammatory research[4][6]. For experimental applications, ACE inhibitors, C-domain-selective inhibitors, and structural ACE-lisinopril complexes support studies of substrate processing, domain selectivity, and cardiovascular drug mechanisms[7][8].- C-domain inhibition helps dissect Ang I-dependent vasoconstriction without blocking all ACE activity[8]. - ACE2 comparisons separate classical ACE signaling from counter-regulatory Ang- (1-7) /Mas-axis mechanisms[6]. - ACE inhibitor models remain useful for cardiovascular, renal, bradykinin, and RAAS pathway studies[2][7].
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Subcellular Localization
Cell membrane; Single-pass type I membrane protein; Cytoplasm; Secreted; Cell membrane; Single-pass type I membrane protein; Secreted
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Expression
Tissue_specificity:It is widely expressed in various tissues throughout the body, with the highest expression levels in the lungs, kidneys, heart, gastrointestinal tract, and prostate; it is specifically expressed in spermatocytes and adult testes.
Induction:Up-regulated in failing heart -
Isoforms & Post-Translational Modification
P12821 has 4 isomers: P12821-1: 149715 Da (predicted); P12821-2: 131659 Da (predicted); P12821-3: 83330 Da (predicted); P12821-4: 78694 Da (predicted).
Produced following proteolytic cleavage by secretase enzymes that cleave the transmembrane form in the juxtamembrane stalk region upstream of the transmembrane region (PubMed:10769174, PubMed:11274151, PubMed:7499427, PubMed:8253769). Cleavage can take place at different sites of the juxtamembrane stalk region (PubMed:10769174, PubMed:11274151, PubMed:7499427, PubMed:8253769);Phosphorylated by CK2 on Ser-1299; which allows membrane retention (PubMed:12386153). Phosphorylated on tyrosine residues on its extracellular part, promoting cleavage by secretase enzymes and formation of the soluble form (Angiotensin-converting enzyme, soluble form) (By similarity) -
Subunit
Monomer and homodimer; homodimerizes following binding to an inhibitor (PubMed:16476786). Interacts with calmodulin (CALM1, CALM2 or CALM3); interaction takes place in the cytoplasmic region and regulates phosphorylation and proteolytic cleavage (By similarity)
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SwissProt ID
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Synonyms
ACE; DCP; DCP1; Angiotensin-converting enzyme; ACE; Dipeptidyl carboxypeptidase I; Kininase II; CD antigen CD143
Documentation
[1]. Masuyer G, et al. Molecular recognition and regulation of human angiotensin-I converting enzyme (ACE) activity by natural inhibitory peptides. Sci Rep. 2012;2:717. [Content Brief]
[2]. Su JB. Different cross-talk sites between the renin-angiotensin and the kallikrein-kinin systems. J Renin Angiotensin Aldosterone Syst. 2014 Dec;15(4):319-28. doi: 10.1177/1470320312474854. Epub 2013 Feb 5. PMID: 23386283. et al. Different cross-talk sites between the renin-angiotensin and the kallikrein-kinin systems. J Renin Angiotensin Aldosterone Syst. 2014 Dec;15(4):319-28. [Content Brief]
[3]. Fuchs S, et al. Angiotensin-converting enzyme C-terminal catalytic domain is the main site of angiotensin I cleavage in vivo. Hypertension. 2008 Feb;51(2):267-74. [Content Brief]
[4]. Rice GI, et al. Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism. Biochem J. 2004 Oct 1;383(Pt 1):45-51. [Content Brief]
[5]. Turner AJ, et al. ACEH/ACE2 is a novel mammalian metallocarboxypeptidase and a homologue of angiotensin-converting enzyme insensitive to ACE inhibitors. Can J Physiol Pharmacol. 2002 Apr;80(4):346-53. [Content Brief]
[6]. Iwai M, et al. Devil and angel in the renin-angiotensin system: ACE-angiotensin II-AT1 receptor axis vs. ACE2-angiotensin-(1-7)-Mas receptor axis. Hypertens Res. 2009 Jul;32(7):533-6. [Content Brief]
[7]. Natesh R, et al. Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature. 2003 Jan 30;421(6922):551-4. [Content Brief]
[8]. van Esch JH, et al. Selective angiotensin-converting enzyme C-domain inhibition is sufficient to prevent angiotensin I-induced vasoconstriction. Hypertension. 2005 Jan;45(1):120-5. [Content Brief]
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