Recombinant Human LCAT Protein (C-6His)

Name: Recombinant Human LCAT Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0707NP
Availability: InStock

BL-0707NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Lecithin-cholesterol Acyltransferase is produced by our Mammalian expression system and the target gene encoding Phe25-Glu440 is expressed with a 6His tag at the C-terminus.
Accession	P04180
Synonym	Phosphatidylcholine-sterol acyltransferase; also named Lecithin-cholesterol acyltransferase; Phospholipid-cholesterol acyltransferase and LACT; is an extracellular cholesterol esterifying enzyme which belongs to the AB hydrolase superfamily.
Gene Background	Lipase family. The gene encoding this protein is expressed mainly in brain, liver and testes,followed by secreting into plasma and cerebral spinal fluid. The esterification of cholesterol is required for cholesterol transport. LCAT is a central enzyme in the extracellular metabolism of plasma lipoproteins. Defects in LCAT are the cause of lecithin-cholesterol acyltransferase deficiency (LCATD) and a cause of fish-eye disease (FED).
Molecular Mass	48.1 KDa
Apmol Mass	66 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 4mM HCl.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target 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.
Subcellular Location	Secreted.
Protein Families	AB hydrolase superfamily, Lipase family
Database References	HGNC: 6522 OMIM: 136120 KEGG: hsa:3931 STRING: 9606.ENSP00000264005 UniGene: 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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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