Angiotensin Converting Enzyme from porcine kidney

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

ACE, Peptidyl-dipeptidase A
CAS Number:
Enzyme Commission number:
MDL number:


lyophilized powder

Quality Level

specific activity

≥10 units/mg protein (Bradford)

shipped in

dry ice

storage temp.


Gene Information

pig ... ACE(613133)

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.


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.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Sequence variation in the human angiotensin converting enzyme
Rieder MJ, et al.
Nature Genetics, 22(1), 59-59 (1999)
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)
Prolyl carboxypeptidase: a forgotten kidney angiotensinase. Focus on "Identification of prolyl carboxypeptidase as an alternative enzyme for processing of renal angiotensin II using mass spectrometry".
Juan Carlos Q Velez
American journal of physiology. Cell physiology, 304(10), C939-C940 (2013-04-05)
Rodrigo A Fraga-Silva et al.
Hypertension (Dallas, Tex. : 1979), 61(6), 1233-1238 (2013-04-24)
Diminished release and function of endothelium-derived nitric oxide coupled with increases in reactive oxygen species production is critical in endothelial dysfunction. Recent evidences have shown that activation of the protective axis of the renin-angiotensin system composed by angiotensin-converting enzyme 2...
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)

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