Human Carboxylesterase 2/CES2 Alexa Fluor™ Plus 488‑conjugated Antibody

Carboxylesterase 2 is a member of a serine esterase family composed of enzymes which hydrolyze ester and amide bonds (1, 2). The members in this family share the serine hydrolase fold observed in other esterases (3). They have broad substrate specificity from small molecule esters such as phenylester to long-chain fatty acid esters and thioesters. They play a major role in the pharmacokinetics of most therapeutic agents containing an ester. By de-esterification, they can activate or inactivate the agents. They also participate in the detoxification of drugs such as cocaine and heroin in serum and liver. In addition to narcotics, they can also detoxify organophosphate and carbamate analogues used in agrochemicals or chemical nerve agents, such as malathion, sarin, tabun, and VX. In addition to the hydrolytic activity, they can perform transesterification. This reaction is important for cholesterol homeostasis. Three major human CESs have been identified (4). CES1 is highly expressed in liver. CES2 is present in the small intestine, colon, kidney, liver, heart, brain, and testis. CES3 is brain-specific. Carboxylesterase deficiency may be associated with non-Hodgkin lymphoma or B-cell lymphocytic leukemia.