Angiotensin I Converting Enzyme (Peptidyl-Dipeptidase A) 1 (ACE) antibody

Antigen: Angiotensin I Converting Enzyme (Peptidyl-Dipeptidase A) 1 (ACE)

Synonyms: DCP, ACE1, DCP1, CD143, MVCD3, MGC26566, AW208573, MGC117827, Dcp1, StsRR92, ACE, LOC100009274, dcp, ace1, dcp1, xace, cd143

Clonality: Monoclonal

Host: Rabbit

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (IHC), Flow Cytometry (FACS)

Certificates: ISO 9001:2008

Catalog no.: ABIN649245

Additional Information

Alternative name: ACE

Gene ID: 1636

UniProt: P12821

Description: Other names: ACE, DCP, DCP1, Angiotensin-converting enzyme, soluble form, Dipeptidyl carboxypeptidase I,Kininase II

Characteristics: Rabbit Monoclonal Antibody

Specificity: A synthetic peptide corresponding to residues on the C-terminus of human ACE was used as an immunogen.

Molecular Weight: 195 kDA

Comments:

Background: Angiotensin-converting enzyme (ACE) is a zinc-containing dipeptidyl carboxypeptidase anchored in the plasma membrane with a carboxy-terminal hydrophobic domain (1, 2). ACE has a critical role in cardiovascular function because it catalyses the conversion of angiotensin I to the physiologically active vasopressor octapeptide angiotensin II, which controls fluid-electrolyte balance and systemic blood pressure (3, 4). Inhibitors of ACE are a first line of therapy for hypertension, heart failure, myocardial infarction and diabetic nephropathy (4). ACE also plays a critical role in the circulating or endocrine renin-angiotensin system (RAS) as well as the local regulation that exists in tissues such as the myocardium and skeletal muscle (5).

Application Details

Application Notes: The suggested dilution is: WB: ~~ 1:1000~10000 FC: ~~ 1:30 IHC: ~~ 1:100~250

Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

Storage: ACE Antibody can be stored at -20°C for up to 12 months from time of receipt.

Research Area: Phospho-specific antibodies, Cell Signaling, Protein Modifications, Cell Structure, Metabolism

Restrictions: For Research Use only

Publications

Product: Ehlers, Fox, Strydom et al.: "Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 86, Issue 20, pp. 7741-5, 1989 (PubMed).

Sugimura, Tian, Hoffmann et al.: "Alternative splicing of the mRNA coding for the human endothelial angiotensin-converting enzyme: a new mechanism for solubilization." in: Biochemical and biophysical research communications, Vol. 247, Issue 2, pp. 466-72, 1998 (PubMed).

Rieder, Taylor, Clark et al.: "Sequence variation in the human angiotensin converting enzyme." in: Nature genetics, Vol. 22, Issue 1, pp. 59-62, 1999 (PubMed).

Natesh, Schwager, Sturrock et al.: "Crystal structure of the human angiotensin-converting enzyme-lisinopril complex." in: Nature, Vol. 421, Issue 6922, pp. 551-4, 2003 (PubMed).

Natesh, Schwager, Evans et al.: "Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin I-converting enzyme." in: Biochemistry, Vol. 43, Issue 27, pp. 8718-24, 2004 (PubMed).