|Detection of Mouse Carboxylesterase 2/CES2 by Western Blot. Western blot shows lysates of mouse liver tissue. PVDF membrane was probed with 1 µg/mL of Goat Anti-Mouse Carboxylesterase 2/CES2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5280) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for Carboxylesterase 2/CES2 at approximately 58-62 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
Carboxylesterase 2 is a member of a large family of carboxylesterases that are responsible for the hydrolysis of ester and amide bonds (1, 2). They have broad substrate specificity ranging from small molecule esters such as phenylester to long-chain fatty acid esters and thioesters. Carboxylesterases play a major role as determinants of pharmacokinetic behavior for most therapeutic agents containing an ester, participating in the detoxification of drugs such as cocaine and heroin in serum and liver. They can also detoxify organophosphate and carbamate analogues used in agrochemicals or chemical nerve agents, such as malathion, sarin, tabun, and VX. Carboxylesterases can also perform transesterification, a reaction important for cholesterol homeostasis. Carboxylesterase deficiency may be associated with non-Hodgkin lymphoma or B-cell lymphocytic leukemia. CES2, also known as acylcarnitine hydrolase M1, shares the serine hydrolase fold observed in other esterases (3). CES2 possesses an endoplasmic reticulum retention signal (HREL) at its C-terminus. The expressed rmCES2 lacks this signal, resulting in its secretion.
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