Product Details

Uniprot No.

Target Names

Alternative Names

Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase), LCAT

Species Reactivity

Human

Immunogen

A synthesized peptide from human LCAT protein

Immunogen Species

Homo sapiens (Human)

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

Rabbit IgG

Clone No.

10F11

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Rabbit IgG in 10mM phosphate buffered saline , pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.

Form

Liquid

Tested Applications

ELISA, IF, FC

Recommended Dilution

Application	Recommended Dilution
IF	1:50-1:200
FC	1:50-1:200

Protocols

ELISA Protocol
Immunofluorescence (IF) Protocol
Flow Cytometry (FC) Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Description

Lecithin-cholesterol acyltransferase (LCAT) serves as a critical enzyme in reverse cholesterol transport, catalyzing the esterification of free cholesterol in plasma lipoproteins. This enzymatic activity is essential for HDL maturation and cholesterol homeostasis, making LCAT a significant target in cardiovascular disease research, lipid metabolism studies, and investigations into familial LCAT deficiency syndromes.

This recombinant monoclonal antibody, clone 10F11, offers researchers the reproducibility and consistency that recombinant technology provides. Because the antibody sequence is defined and produced in a controlled expression system, you can expect uniform performance across experiments and over time, eliminating the lot-to-lot variability that can complicate long-term studies or multi-site collaborations. The rabbit host origin combined with monoclonal specificity ensures high-affinity binding to human LCAT.

Validation studies demonstrate reliable performance in both immunofluorescence and flow cytometry applications. Immunofluorescence staining of HeLa cells at dilutions between 1:50 and 1:200 reveals clear cytoplasmic localization patterns when combined with appropriate fixation and permeabilization protocols. Flow cytometric analysis using K562 cells shows distinct positive population shifts compared to isotype controls, confirming the antibody's utility for quantitative single-cell analysis of LCAT expression. The antibody has also been validated for ELISA applications, providing additional flexibility for researchers requiring plate-based detection methods.

Whether you are investigating cholesterol metabolism pathways, characterizing LCAT expression in disease models, or screening for modulators of reverse cholesterol transport, this antibody provides a dependable tool for your research. Its validated performance across multiple detection platforms supports diverse experimental approaches in lipid biology and metabolic disease research.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

Target Background

Function

Central enzyme in the extracellular metabolism of plasma lipoproteins. Synthesized mainly in the liver and secreted into plasma where it converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LDLs). The cholesterol ester is then transported back to the liver. Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines. Also produced in the brain by primary astrocytes, and esterifies free cholesterol on nascent APOE-containing lipoproteins secreted from glia and influences cerebral spinal fluid (CSF) APOE- and APOA1 levels. Together with APOE and the cholesterol transporter ABCA1, plays a key role in the maturation of glial-derived, nascent lipoproteins. Required for remodeling high-density lipoprotein particles into their spherical forms. Catalyzes the hydrolysis of 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet-activating factor or PAF) to 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF). Also catalyzes the transfer of the acetate group from PAF to 1-hexadecanoyl-sn-glycero-3-phosphocholine forming lyso-PAF. Catalyzes the esterification of (24S)-hydroxycholesterol (24(S)OH-C), also known as cerebrosterol to produce 24(S)OH-C monoesters.

Gene References into Functions

It has been found a significant association between LCAT serum activity and risk of diabetes mellitus in men but not in women. PMID: 30055622
Single Nucleotide Polymorphism in LCAT gene is associated with dyslipidemia. PMID: 29758034
data suggests a model wherein the active site of LCAT is shielded from soluble substrates by a dynamic lid until it interacts with HDL to allow transesterification to proceed PMID: 29030428
Increased LCAT activity may be associated with increased formation of triglyceride rich lipoproteins, leading to a reduction in LDL particle size and atherosclerosis. PMID: 25894629
Mapping the naturally occurring mutations onto the structure provides insight into how they may affect LCAT enzymatic activity. PMID: 26195816
Report slightly reduction in LCAT that would probably reflect a delay in reverse cholesterol transport occurring in MetS. PMID: 26232163
rs5923 polymorphism is not associated with low high-density lipoprotein cholesterol(HDL-C)levels in Iranian population PMID: 26117245
increased cholesterol esterification by LCAT is atheroprotective PMID: 25964513
The data indicate that this novel apoA-I missense is associated with markedly decreased levels of HDL cholesterol and very large alpha-1 HDL, as well as decreased serum cellular cholesterol efflux and LCAT activity PMID: 26073399
A robust all-atom model for LCAT generated by homology modeling PMID: 25589508
genetic polymorphism is associated with coronary artery disease in Egyptians PMID: 25110219
This study investigated how the natural LCAT[T147I] and LCAT[P274S] mutations affect the pathway of biogenesis of high-density lipoproteins. PMID: 25948084
A synonymous H287H mutation in the coding region of exon 6 of the lecithin cholesterol acyltransferase gene was observed in an individual with HDLC levels of 75 mg/dl. PMID: 24789697
Cosyntropin testing in an unselected subgroup of 8 ABCA1 mutation carriers and 3 LCAT mutation carriers did not reveal differences between carriers and controls. PMID: 24842300
The enzyme lecithin-cholesterol acyltransferase esterifies cerebrosterol and limits its toxic effect on cultured neurons. PMID: 24620755
Activity of LCAT in HDL was increased in type 2 diabetes following increased fruit and vegetable intake. PMID: 24423117
Results show that recombinant lecithin:cholesterol acyltransferase rhLCAt efficiently reduces the amount of unesterified cholesterol and promotes the production of plasma cholesteryl esters in LCAT deficient plasma. PMID: 24140107
The present study provides an important insight into the potential interactions between LCAT and lipoproteins and also suggests that peptides, initially present in a disordered conformation, are able to sense the lipid environment provided by lipoproteins of plasma and following a disorder-to-order transition, change their conformation to an ordered alpha-helix. PMID: 24383078
Male soccer players had significantly higher lecithin-cholesterol acyltransferase activity than sedentary controls. PMID: 23152129
a novel function of apoA-IV in the biogenesis of discrete HDL-A-IV particles with the participation of ABCA1 and LCAT PMID: 23132909
Pulse wave velocity is increased in LCAT mutation carriers with low HDL-c and is associated with carotid wall thickening. PMID: 23078883
carriers of LCAT mutations present with significant reductions in LCAT activity, HDL cholesterol, apoA-I, platelet-activating factor-acetylhydrolase activity and antioxidative potential of HDL, but this is not associated with parameters of increased lipid peroxidation PMID: 23023370
while LCAT activity is decreased in patients with T2DM, LCAT levels is increased. Patients with NIDDM exhibit opposing effects on LCAT activity and LCAT production which is more severe in women PMID: 23142243
Studies suggest that absence of lecithin cholesterol acyltransferase (LCAT) may protect against insulin resistance, diabetes and obesity. PMID: 22326749
mutations in ABCA1, APOA1, and LCAT are sufficient to explain more tha 40 percent of familial hypoalphalipoproteinemia PMID: 21875686
This review focuses on mutations in the LCAT gene as cause of familial hypoalphalipoproteinemia, and on their impact on plasma HDL-C, HDL profile and coronary heart disease. PMID: 22189200
Studies indicate the direct effects of HDL and its major modulators, ATP-binding cassette transporter A1 (ABCA1), apolipoprotein A-I (ApoA-I), and lecithin cholesterol acyltransferase (LCAT) on the development of type 2 diabetes mellitus (T2D). PMID: 22418575
functional mutations in LCAT were found in 29% of patients with low HDL-c, thus constituting a common cause of low HDL-c in referred patients in The Netherlands (LCAT) PMID: 21901787
Low plasma HDL cholesterol levels robustly associated with increased risk of MI but genetically decreased HDL cholesterol did not. PMID: 22090275
Continuous and intermittent walking alters HDL(2)-C and LCATa PMID: 21798542
AAV8-mediated overexpression of human LCAT in hCETP/Ldlr(+/-) mice resulted in profound changes in plasma lipid profiles. PMID: 21822774
Carriers of LCAT gene mutations exhibit increased carotid atherosclerosis PMID: 22133847
analysis of a mutation that causes a complete loss of catalytic activity of LCAT, which is also defective in secretion [case report] PMID: 21597230
LCAT activity and enzyme levels were significantly lower among subjects with low HDL-C compared with subjects with high HDL-C. PMID: 21600519
Case Report: familial LCAT deficienty can cause nephropathy at a very early age. PMID: 21315357
Novel N-terminal mutation of human apolipoprotein A-I reduces self-association and impairs LCAT activation PMID: 20884842
LCAT activity is significantly decreased in type 2 diabetes. The lower LCAT activity in type 2 diabetes might be through ox-LDL mechanism. Ox-LDL may adversely affect high-density lipoprotein -cholesterol metabolism by reducing LCAT activity. PMID: 20890173
Plasma lecithin: cholesterol acyltransferase activity modifies the inverse relationship of C-reactive protein with HDL cholesterol in nondiabetic men. PMID: 19800416
lecithin:cholesterol acyltransferase activity is not responsible for low incidence of cardiovascular events PMID: 19698944
Low LCAT plasma levels are not associated with increased atherosclerosis in the general population. PMID: 19671930
Suggest that a LCAT-/- genotype associated with an APOE epsilon2 allele could be a novel mechanism leading to dysbetalipoproteinemia in familial LCAT deficient patients. PMID: 19515369
The lecithin:cholesterol acyltransferase (LCAT) activity in cord blood was extremely low. PMID: 11882335
Results suggest that LCAT may take part in the detoxification of oxidants even after the loss of its cholesterol esterification function. PMID: 11966470
IL-6 induced activation of full-length LCAT promoter activity. A minimal IL-6 response element mapped within the distal promoter and was sufficient to mediate the IL-6 response PMID: 12032172
In conclusion, 12% of Hypoalphalipoproteinemia subjects were found to carry mutations in apo A-I, LCAT, or GBA genes PMID: 12048121
The results suggest that as follicle maturation progresses, Toc and Asc concentrations increase in follicular fluid, thus protecting LCAT from oxidative damage and loss of activity PMID: 12051518
Endotoxin-lipoprotein complex formation as a factor in atherogenesis: associations with hyperlipidemia and with lecithin:cholesterol acyltransferase activity PMID: 12139471
comparison of 5 natural point mutations of apo A-I illustrates that a specific sequence between amino acids 110 and 162 is required for LCAT activation PMID: 12573451
608T polymorphism of LCAT gene was associated with higher plasma HDL-C level in Coronary Arteriosclerosis patients. PMID: 12673583
Familial lecithin:cholesterol acyltransferase (LCAT) deficiency, arising from mutation, is associated with complete absence of Lecithin:cholesterol acyltransferase (LCAT) activity. PMID: 12957688

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Involvement in disease

Lecithin-cholesterol acyltransferase deficiency (LCATD); Fish-eye disease (FED)

Subcellular Location

Secreted.

Protein Families

AB hydrolase superfamily, Lipase family

Tissue Specificity

Detected in blood plasma. Detected in cerebral spinal fluid (at protein level). Detected in liver. Expressed mainly in brain, liver and testes.

Database Links

HGNC: 6522

OMIM: 136120

KEGG: hsa:3931

STRING: 9606.ENSP00000264005

UniGene: Hs.387239

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Code	CSB-RA261042A0HU
Size	US$210
	Order now
Image	Immunofluorescence staining of Hela cell with CSB-RA261042A0HU at 1:50, counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeabilized using 0.2% Triton X-100 and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L). Overlay Peak curve showing K562 cells stained with CSB-RA261042A0HU (red line) at 1:100. The cells were fixed in 4% formaldehyde and permeated by 0.2% TritonX-100 for 10min. Then 10% normal goat serum to block non-specific protein-protein interactions followed by the antibody (1ug/110⁶cells) for 45min at 4℃. The secondary antibody used was FITC-conjugated goat anti-rabbit IgG (H+L) at 1/200 dilution for 35min at 4℃.Control antibody (green line) was Rabbit IgG (1ug/110⁶cells) used under the same conditions. Acquisition of >10,000 events was performed.
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LCAT Recombinant Monoclonal Antibody

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Target Background