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A2580

Sigma-Aldrich

Angiotensin Converting Enzyme from porcine kidney

lyophilized powder, ≥10 units/mg protein (Bradford)

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Synonym(s):
ACE, Peptidyl-dipeptidase A
CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.32

form

lyophilized powder

Quality Level

specific activity

≥10 units/mg protein (Bradford)

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

pig ... ACE(613133)

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This Item
A6778SAE0075A3010
specific activity

≥10 units/mg protein (Bradford)

specific activity

≥2.0 units/mg protein (modified Warburg-Christian)

specific activity

≥10 U/mg

specific activity

≥1500 units/mg protein

UniProt accession no.

A0A480IQM9

UniProt accession no.

-

UniProt accession no.

P12821

UniProt accession no.

P37111

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

shipped in

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

General description

ACE is a monomer with molecular weight of ~170 kDa
pH range for activity: 7-8.5
Temperature optimum: 37 °C
Zinc is required for activity
Inhibitors: captopril, enalaprilat, lisinopril etc. (1-10 μM)
Angiotensin converting enzyme (ACE) is encoded by the gene, mRNA-decapping enzyme subunit 1 (DCP1). It is a zinc metalloprotease, which belongs to the M2 family.

Application

Angiotensin converting enzyme from porcine kidney has been used in in vitro angiotensin-converting enzyme (ACE) inhibition assay.

Biochem/physiol Actions

Angiotensin converting enzyme (ACE) catalyzes the conversion of angiotensin I to angiotensin II, which regulates the fluid-electrolyte balance and systemic blood pressure. ACE inhibits the vasodilator, bradykinin. ACE inhibitors are used to treat high blood pressure.
Removes C-terminal dipeptides from susceptible substrates, e.g., angiotensin I and bradykinin.

Unit Definition

One unit will produce 1.0 ·μmole of hippuric acid from Hippuryl-His-Leu per min in 50 mM HEPES and 300 mM NaCl at pH 8.3 at 37 °C.

Physical form

Lyophilized powder containing Tris buffer salts.

inhibitor

Product No.
Description
Pricing

substrate

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Customers Also Viewed

Sequence variation in the human angiotensin converting enzyme
Rieder MJ, et al.
Nature Genetics, 22(1), 59-59 (1999)
A Human Homolog of Angiotensin Converting Enzyme-Cloning and Functional Expression As A Captopril Insensitive Carboxypeptidase
Tipnis SR, et al.
The Journal of Biological Chemistry (2000)
Evaluation of mechanism for antihypertensive action of Clerodendrum colebrookianum Walp., used by folklore healers in north-east India
Lokesh D and Amitsankar D
Journal of Ethnopharmacology, 143(1), 207-212 (2012)
N M Hooper et al.
The Biochemical journal, 241(3), 625-633 (1987-02-01)
Peptidyl-dipeptidase A (angiotensin converting enzyme; ACE, EC 3.4.15.1), has been purified from pig kidney and striatum by affinity chromatography employing the selective inhibitor lisinopril as ligand. The inclusion of a 2.8 nm spacer arm improved the yield of the enzyme
Effect of angiotensin-converting-enzyme inhibition compared with conventional therapy on cardiovascular morbidity and mortality in hypertension: the Captopril Prevention Project (CAPPP) randomised trial
Hansson L, et al.
Lancet, 353(9153), 611-616 (1999)

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