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Manufactured by BioVendor

Lecithin-Cholesterol Acyltransferase Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:LCAT, Phosphatidylcholine-sterol acyltransferase, Phospholipid-cholesterol acyltransferase
  • Species:Human
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Cat. No. Size Price


RD191122200R 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, Biotin-labelled antibody

Applications

Serum, Plasma-EDTA, Plasma-Citrate, Cerebrospinal fluid

Sample Requirements

serum and plasma: 5µl/well
CSF: 10µl/well

Shipping

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

Storage/Expiration

Store the complete kit at 2–8°C. Under these conditions, the kit is stable until the expiration date (see label on the box).

Calibration Curve

Calibration Range

2.5–160 ng/ml

Limit of Detection

0.27 ng/ml

Intra-assay (Within-Run)

n = 8; CV = 2.6%

Inter-assay (Run-to-Run)

n = 6; CV = 5.9%

Spiking Recovery

97,40%

Dilution Linearity

102,80%

Crossreactivity

  • bovine Non-detectable
  • cat Non-detectable
  • dog Non-detectable
  • goat Non-detectable
  • hamster Non-detectable
  • horse Non-detectable
  • human Non-detectable
  • chicken Non-detectable
  • pig Non-detectable
  • rabbit Non-detectable
  • rat Non-detectable
  • sheep Non-detectable
  • monkey Yes
  • mouse Yes
Summary

Features

  • It is intended for research use only
  • The total assay time is less than 3.5 hours
  • The kit measures LCAT in serum, plasma (EDTA, citrate) and cerebrospinal fluid (CSF)
  • Assay format is 96 wells
  • Standard is recombinant protein based
  • Quality Controls are human serum based
  • Components of the kit are provided ready to use, concentrated or lyophilized

Research topic

Cardiovascular disease, Lipoprotein metabolism

Summary

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.

Product References (2)

References

  • Freeman LA, Demosky SJ Jr, Konaklieva M, Kuskovsky R, Aponte A, Ossoli AF,Gordon SM, Koby RF, Manthei KA, Shen M, Vaisman BL, Shamburek RD, Jadhav A,Calabresi L, Gucek M, Tesmer JJG, Levine RL, Remaley AT. Lecithin:CholesterolAcyltransferase Activation by Sulfhydryl-Reactive Small Molecules: Role ofCysteine-31. J Pharmacol Exp Ther. 2017 Aug;362(2):306-318. doi:10.1124/jpet.117.240457. Epub 2017 Jun 2. PubMed PMID: 28576974; PubMed CentralPMCID: PMC5510151. See more on PubMed
  • Greenwald P, Kirmss V, Burnett WS. Prostate cancer epidemiology: widowerhoodand cancer in spouses. J Natl Cancer Inst. 1979 May;62(5):1131-6. PubMed PMID:286088. See more on PubMed
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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