| Product Name | LCAT, 25-440aa, Human |
|---|---|
| Description | LCAT (lecithin-cholesterol acyltransferase), also known as phosphatidylcholine-sterol O-acyltransferase, belongs to the AB hydrolase superfamily. LCAT is responsible for the esterification of the free cholesterol of plasma lipoproteins. This enzyme is converts free cholesterol into cholesteryl ester (a more hydrophobic form of cholesterol), which is then sequestered into the core of a lipoprotein particle, eventually making the newly synthesized HDL spherical and forcing the reaction to become unidirectional since the particles are removed from the surface. It is central enzyme in the extracellular metabolism of plasma lipoproteins and required for remodeling high-density lipoprotein particles into their spherical forms. Recombinant human LCAT protein, fused to His-tag at N-terminus, was expressed in E.coli. |
| Synonyms | Phosphatidylcholine-sterol acyltransferase, lecithin-cholesterol acyltransferase, phosphatidylcholine-sterol O-acyltransferase |
| Host | E.coli |
| Molecular Weight | 38.7kDa (345aa) |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSHMFWLLN VLFPPHTTPK AELSNHTRPV ILVPGCLGNQ LEAKLDKPDV VNWMCYRKTE DFFTIWLDLN MFLPLGVDCW IDNTRVVYNR SSGLVSNAPG VQIRVPGFGK TYSVEYLDSS KLAGYLHTLV QNLVNNGYVR DETVRAAPYD WRLEPGQQEE YYRKLAGLVE EMHAAYGKPV FLIGHSLGCL HLLYFLLRQP QAWKDRFIDG FISLGAPWGG SIKPMLVLAS GDNQGIPIMS SIKLKEEQRI TTTSPWMFPS RMAWPEDHVF ISTPSFNYTG RDFQRFFADL HFEEGWYMWL QSRDLLAGLP APGVEVYCLY GVGLPTPRTY IYDHGFPYTD PVGVLYEDGD DTVATRSTEL CGLWQGRQPQ PVHLLPLHGI QHLNMVFSNL TLEHINAILL GAYRQGPPAS PTASPEPPPP E |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 0.4M urea, 10% glycerol |
| Concentration | 1 mg/ml (determined by Bradford assay) |
| Purity | >85% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -20C or -70C. Avoid repeated freezing and thawing cycles. |
| References |
Clay M.A., et al. (2000) J. Biol. Chem. 275:9019-9025 Karavia EA, et al. (2012) J Nutr Biochem. 2012 Jul 19. |
| Supplier | ARP |
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