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Manufactured by BioVendor

Lecithin-Cholesterol Acyltransferase Human HEK293

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:HEK293
  • Other names:LCAT, Phosphatidylcholine-sterol acyltransferase, Phospholipid-cholesterol acyltransferase
  • Species:Human
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Cat. No. Size Price

RD172122100-HEK 0.1 mg
PubMed Product Details
Technical Data


Recombinant protein


Total 429 AA. MW: 48.5 kDa (calculated). UniProtKB/Swiss-Prot P04180 Phe25-Glu440 with N-Terminal Flag-tag, 13 extra AA (highlighted).

Amino Acid Sequence





Purity as determined by densitometric image analysis: >95%


14% SDS-PAGE separation of Human LCAT
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and heated sample, 5μg/lane
3. non-reduced and non-heated sample, 5μg/lane


< 0.1 EU/μg


Filtered (0.4 μm) and lyophilized from 0.5 mg/ml in 20mM Tris buffer, 50mM NaCl, pH 7.5


Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.


Western blotting, ELISA, Cell culture and/or animal studies


At ambient temperature. Upon receipt, store the product at the temperature recommended below.


Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.


This product is intended for research use only.


Research topic

Cardiovascular disease, Lipoprotein metabolism


Human Lecithin: cholesterol acyltransferase (LCAT) is a glycoprotein with a molecular mass of approximately 58 kDa. It is the key enzyme responsible for esterification of free cholesterol to cholesteryl esters in circulating plasma lipoproteins, primarily in high density lipoprotein (HDL). The tertiary structure of LCAT is maintained by two disulfide bridges, similar to lipases and other proteins of the α/β hydrolase fold family. Mature LCAT protein is synthesized from a 440 residue precursor by following cleavage of a 24 residue signal peptide. The mature protein contains 416 amino acids and is heavily N-glycosylated. LCAT is abundant in blood plasma and it is present in other organs, including liver, brain and testes. In plasma LCAT is associated with ApoD which frequently co-purify. A recent study suggests that LCAT can act as an antioxidant and prevent the accumulation of oxidized lipid in plasma lipoproteins. LCAT performs a central role in HDL metabolism by catalyzing the formation of cholesteryl esters on HDL through the transfer of fatty acids from the sn-2 positions of phosphatidylcholine (PC) to cholesterol. The role of LCAT in atherosclerosis is unclear. Dullaart et al. showed that plasma LCAT activity is elevated in metabolic syndrome and may be a marker of subclinical atherosclerosis. Sethi et al. demonstrated that low lecithin-cholesterol acyltransferase (LCAT) activities and high pre-ß1-HDL concentrations are strong positive risk markers for ischemic heart disease and are independent of HDLcholesterol. Miida et al. demonstrated that plasma pre β1-HDL concentration increase in subjects with low LCAT activity. They also reported that patients with coronary artery diseae (CAD) had higher pre-ß1-HDL concentrations than did normolipidemic subjects. Holleboom et al. showed that low plasma LCAT levels (reflecting low LCAT activity) are not associated with an increased risk of future (CAD) in the general population. However, other studies showed a positive association of LCAT levels with carotid atherosclerosis in patients with the metabolic syndrome as well as in control subjects whereas, LCAT activity was reduced in patients with CAD and in patients with acute myocardial infarction. In summary, LCAT activity might be reduced in the acute phase of a myocardial infarction. Mutations of LCAT on chromozome 16 resulting in homozygous or compound heterozygous form can cause two major phenotypes: FLD (familial LCAT deficiency) and FED ( Fish Eye Disease). Patients with FLD have a complete loss of both α-LCAT activity and β-LCAT activity and an increased proportion of unesterified cholesterol in plasma. In FED is partial loss of α-LCAT activity with normal elevated free cholesterol in plasma. Both FLD and FED are characterized by the development of corneal opacities.

Summary References (9)

References to Lecithin-Cholesterol Acyltransferase

  • Berard AM, Clerc M, Brewer B Jr, Santamarina-Fojo S. A normal rate of cellular cholesterol removal can be mediated by plasma from a patient with familial lecithin-cholesterol acyltransferase (LCAT) deficiency. Clin Chim Acta. 2001 Dec;314 (1-2):131-9
  • Charlton-Menys V, Pisciotta L, Durrington PN, Neary R, Short CD, Calabresi L, Calandra S, Bertolini S. Molecular characterization of two patients with severe LCAT deficiency. Nephrol Dial Transplant. 2007 Aug;22 (8):2379-82
  • Dullaart RP, Perton F, Sluiter WJ, de Vries R, van Tol A. Plasma lecithin: cholesterol acyltransferase activity is elevated in metabolic syndrome and is an independent marker of increased carotid artery intima media thickness. J Clin Endocrinol Metab. 2008 Dec;93 (12):4860-6
  • Holleboom AG, Kuivenhoven JA, Vergeer M, Hovingh GK, van Miert JN, Wareham NJ, Kastelein JJ, Khaw KT, Boekholdt SM. Plasma levels of lecithin:cholesterol acyltransferase and risk of future coronary artery disease in apparently healthy men and women: a prospective case-control analysis nested in the EPIC-Norfolk population study. J Lipid Res. 2010 Feb;51 (2):416-21
  • Miida T, Obayashi K, Seino U, Zhu Y, Ito T, Kosuge K, Hirayama S, Hanyu O, Nakamura Y, Yamaguchi T, Tsuda T, Saito Y, Miyazaki O, Nakamura Y, Okada M. LCAT-dependent conversion rate is a determinant of plasma prebeta1-HDL concentration in healthy Japanese. Clin Chim Acta. 2004 Dec;350 (1-2):107-14
  • Rousset X, Vaisman B, Amar M, Sethi AA, Remaley AT. Lecithin: cholesterol acyltransferase--from biochemistry to role in cardiovascular disease. Curr Opin Endocrinol Diabetes . 2009 Apr;16 (2):163-71
  • Rousset X, Vaisman B, Auerbach B, Krause BR, Homan R, Stonik J, Csako G, Shamburek R, Remaley AT. Effect of recombinant human lecithin cholesterol acyltransferase infusion on lipoprotein metabolism in mice. J Pharmacol Exp Ther. 2010 Oct;335 (1):140-8
  • Sethi AA, Sampson M, Warnick R, Muniz N, Vaisman B, Nordestgaard BG, Tybjaerg-Hansen A, Remaley AT. High pre-beta1 HDL concentrations and low lecithin: cholesterol acyltransferase activities are strong positive risk markers for ischemic heart disease and independent of HDL-cholesterol. Clin Chem. 2010 Jul;56 (7):1128-37
  • Tanigawa H, Billheimer JT, Tohyama J, Fuki IV, Ng DS, Rothblat GH, Rader DJ. Lecithin: cholesterol acyltransferase expression has minimal effects on macrophage reverse cholesterol transport in vivo. Circulation. 2009 Jul 14;120 (2):160-9
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