CES1, Recombinant, Mouse, aa19-565, His-tag (Carboxylesterase 1, ACAT, Egasyn, HMSE1, REH, SES1, TGH)

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 deпїЅesterification, 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 deпїЅesterified 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 nonпїЅHodgkin lymphoma or BпїЅcell lymphocytic leukemia. CESпїЅ1 shares the serine hydrolase fold observed in other esterases (3). Ces1G is a rat and mouse specific protein that is expressed predominantly in liver, but also in kidney and lung (4).\n\nSource:\nRecombinant protein corresponding to aa19-565 from mouse Carboxylesterase 1/CES1, fused to his-tag at C-terminal, NS0-derived.\n\nMolecular Weight: \n~55-60kD\n\nEndotoxin:\n<1.0EU/1ug (LAL method).\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

145782

Size

20ug

Form

Supplied as a liquid in Tris, NaCl. BSA free.

Purity

~90% (SDS-PAGE)

References

1. Redinbo, M.R. and Potter, P.M. (2005) Drug Discovery Today 10:313. 2. Satoh, T. and Hosokawa, M. (2006) Chem. Biol. Interactions 162:195. 3. Fleming, C.D. et al. (2007) Biochemistry 46:5603. 4. Ellinghaus P. et al. (1998) Biochim. Biophys. Acta. 1397:175.