>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<1.0 EU per 1 μg of the protein by the LAL method.
61 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Carboxylesterase 1 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. They play a major role as determinants of pharmacokinetic behavior for most therapeutic agents containing an ester. By de-esterification, they can activate or inactivate the agents. They also participate in detoxification of drugs such as cocaine and heroin in serum and liver. The resulting de-esterified metabolites are secreted out in urine. 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, a reaction important for cholesterol homeostasis. Carboxylesterase deficiency may be associated with non-Hodgkin lymphoma or B-cell lymphocytic leukemia. CES-1 shares the serine hydrolase fold observed in other esterases (3). CES-1 possesses an endoplasmic reticulum retention signal (HIEL) at its C-terminus. The purified rhCES-1 lacks this signal, resulting in its secretion.
Redinbo, M. R. and Potter, P.M. (2005) Drug Discovery Today 10:313.
Satoh, T. and Hosokawa, M. (2006) Chem. Biol. Interactions 162:195.
Fleming, C. D. et al. (2007) Biochemistry 46:5603.
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