ACE (kininase II, EC 3.4.15.1) is a zinc dipeptidyl carboxypeptidase. ACE catalyses both angiotensin I transformation to angiotensis II (a potent vasopressor agent) and degradation of bradikinin, a vaso-depressor. ACE appears to play a key role in regulating vascular tone and remodeling the development of atherosclerotic lesions. Increasing evidence suggests that ACE plays an important role in vascular pathology. Recent studies shows two new functions of this important enzyme: 1) It enhances the presentation of endogenous antigens (in particularly HIV 1 gp160-derived peptide p18) to MHC class I-restricted T-lynphocytes (ref. 1); 2) Its amino-terminal domain cleaves effectively hemoregulatory tetrapeptide N-Ac-Ser-Asp-Lys-Pro (ref. 2,3) which is involved in the control of hemapoetic stem cell proliferation (the amount of this peptide greatly decreases in patients undergoing cancer chemotherapy) (ref. 4).

Product Source: Isolated from rat lung using affinity chromatography (ref. 5).

As a reference in SDS-PAGE and Western blotting [together with anti-ACE monoclonal (MAB4051) also available from Chemicon]. For Western blotting 500 ng/lane if gel is developed with anti-ACE MAB4051.

As a reference antigen for immunoprecipitation of ACE from various tissue samples (in combination with anti-ACE MAB4051).

As a source of pure ACE for different enzymatic studies of ACE (testing of ACE inhibitors, substrate specificity, kinetic measurements, etc.).

Optimal working concentration must be determined by the end user.

Specific Activity: One unit will produce 1 μmoL of hippuric acid or His-Leu from Z-Phe-His-Leu per minute in 0.1 M phosphate buffer and 300 mM NaCl at pH 8.3 at 37°C.

Liquid in 100 mM phosphate buffered saline, 150 mM NaCl, pH 7.4 with 0.2mM CHAPS. Purity is >95% by SDS-PAGE when 10 μg was loaded. Contains no preservative.

Concentration: Refer to Certificate of Analysis for each individual lot of this enzyme.

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