Product category:
Clinical chemistry analysis
News Release from: Cambridge BioScience | Subject: Nat1 and Nat2
Edited by the Laboratorytalk Editorial
Team on 13 March 2003
New tools for HTS drug metabolism
studies
Baculovirus expressed human Nat1 and Nat2 preparations enable the study of soluble drug metabolising enzymes in the cytosol, facilitating the final stages of ADME profiling
Cambridge Bioscience has introduced two unique new tools for drug metabolism studies in a high-throughput environment Developed by BD Gentest, the baculovirus expressed human Nat1 and Nat2 preparations enable the study of soluble drug metabolising enzymes in the cytosol, facilitating the final stages of ADME profiling
This article was originally published on Laboratorytalk on 4 Jul 2005 at 8.00am (UK)
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Unlike P450 enzymes, the Nat1 and Nat2 proteins are not membrane-bound and play a significant role in drug metabolism.
Arylamine N-acetyltransferases (Nats) are cytosolic proteins expressed in a variety of tissues.
In humans there are two functional isoforms: Nat1 and Nat2.
Nat1 has a ubiquitous tissue distribution; Nat2 is distributed primarily in the liver and intestine.
In addition to playing a key role in the N-acetylation of drugs, Nat enzymes also contribute to the metabolic activation of xenobiotics.
These include cigarette smoke and carcinogens found in cooked foods.
Several polymorphisms have been reported, particularly Nat2.
BD Gentest's Nat1 and Nat2 are derived from 'wild type' alleles, Nat1*4 and Nat2*4.
The enzymes are prepared from the cytosolic (soluble) fraction of insect cells infected with recombinant baculovirus.
A control insect cell cytosolic preparation is also available.
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