Analytical Data
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基因名
LCAT
- Application
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别名
phosphatidylcholine-sterol O-acyltransferase; Phospholipid-cholesterol acyltransferase
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
P04180
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表达区间
Glu41~His210
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分子量
23kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
LCAT, or lecithin-cholesterol acyltransferase, is a crucial enzyme in lipid metabolism, primarily responsible for the conversion of free cholesterol into cholesteryl esters, which are subsequently transported in lipoproteins. The significance of LCAT in cardiovascular health is highlighted by its role in the reverse cholesterol transport pathway, where it aids in the removal of excess cholesterol from peripheral tissues and its delivery to the liver for excretion. Dysregulation of LCAT activity has been associated with various lipid disorders, including high-density lipoprotein (HDL) dysfunction and atherosclerosis, making it a target for therapeutic interventions. Research into recombinant LCAT (rLCAT) has gained momentum as scientists aim to better understand its structure-function relationships and to develop potential biotherapeutics for dyslipidemia and related cardiovascular diseases. By employing recombinant DNA technology, researchers can produce LCAT in vitro, allowing for detailed biochemical analyses and the exploration of its enzymatic mechanisms. This has led to increased interest in potential strategies to enhance LCAT activity or to develop LCAT mimetics, which could help in mitigating the effects of cardiovascular diseases linked to lipid imbalances. As the prevalence of cardiovascular diseases rises worldwide, LCAT represents a promising avenue for innovative treatments, emphasizing the importance of ongoing research in this domain.
