ACE Antibody (YA2094)(PBS only)
(Synonyms: ACE; Dipeptidyl carboxypeptidase I; Kininase II; Angiotensin Converting Enzyme 1 Antibody )ACE Antibody (YA2094) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to ACE.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P
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Reactivity :
Mouse, Rat
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Formulation:
Supplied in PBS, pH 7.4.
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Conjugation:
Non-conjugated
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Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|---|
| Dilution Ratio | 1:500-1:1000 | 1:50-1:100 |
Product Details
ACE Antibody (YA2094) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to ACE.
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Host Rabbit
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Species ReactivityMouse, Rat
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Observed Molecular WeightObserved band size: 180 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 151 kDa
Recombinant protein of mouse Angiotensin Converting Enzyme 1 aa636 -1237.
Affinity Purified
Non-conjugated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, pH 7.4.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
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:Highly expressed in the kidneys and lungs; not expressed in the liver (PubMed:16154999) . In the brain, expressed in the cerebral cortex, hippocampus, cerebellum, and basal ganglia/brainstem (PubMed:16154999) . Highly expressed in neurons of the dopamine receptor DRD1 in the dorsal striatum and nucleus accumbens (PubMed:35201898) ; specifically expressed in spermatocytes and adult testes. -
Isoforms & Post-Translational Modification
P09470 has 2 isomers: P09470-1: 150918 Da (predicted); P09470-2: 84047 Da (predicted).
Produced following proteolytic cleavage by secretase enzymes that cleave the transmembrane form in the juxtamembrane stalk region upstream of the transmembrane region. Cleavage can take place at different sites of the juxtamembrane stalk region;Phosphorylated by CK2 on Ser-1305; which allows membrane retention (By similarity). 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 (By similarity). 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; Dipeptidyl carboxypeptidase I; Kininase II; Angiotensin Converting Enzyme 1 Antibody
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Research Field
Cardiovascular
Documentation
References
[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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