Analytical Data
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基因名
LSS
- Application
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别名
LSS；OSC；Lanosterol synthase
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P48449
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表达区间
2-732aa
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氨基酸序列
TEGTCLRRRGGPYKTEPATDLGRWRLNCERGRQTWTYLQDERAGREQTGLEAYALGLDTKNYFKDLPKAHTAFEGALNGMTFYVGLQAEDGHWTGDYGGPLFLLPGLLITCHVARIPLPAGYREEIVRYLRSVQLPDGGWGLHIEDKSTVFGTALNYVSLRILGVGPDDPDLVRARNILHKKGGAVAIPSWGKFWLAVLNVYSWEGLNTLFPEMWLFPDWAPAHPSTLWCHCRQVYLPMSYCYAVRLSAAEDPLVQSLRQELYVEDFASIDWLAQRNNVAPDELYTPHSWLLRVVYALLNLYEHHHSAHLRQRAVQKLYEHIVADDRFTKSISIGPISKTINMLVRWYVDGPASTAFQEHVSRIPDYLWMGLDGMKMQGTNGSQIWDTAFAIQALLEAGGHHRPEFSSCLQKAHEFLRLSQVPDNPPDYQKYYRQMRKGGFSFSTLDCGWIVSDCTAEALKAVLLLQEKCPHVTEHIPRERLCDAVAVLLNMRNPDGGFATYETKRGGHLLELLNPSEVFGDIMIDYTYVECTSAVMQALKYFHKRFPEHRAAEIRETLTQGLEFCRRQQRADGSWEGSWGVCFTYGTWFGLEAFACMGQTYRDGTACAEVSRACDFLLSRQMADGGWGEDFESCEERRYLQSAQSQIHNTCWAMMGLMAVRHPDIEAQERGVRCLLEKQLPNGDWPQENIAGVFNKSCAISYTSYRNIFPIWALGRFSQLYPERALAGHP
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分子量
89.2 kDa
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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
LSS, or lanosterol synthase, is a crucial enzyme in the cholesterol biosynthesis pathway, catalyzing the conversion of squalene to lanosterol, a precursor of sterols. The study of LSS-recombinant proteins has gained significant interest due to its implications in various biological processes and disease states, particularly in the context of metabolic disorders and cardiovascular diseases. Genetic mutations affecting LSS activity can lead to conditions such as congenital lipoid adrenal hyperplasia, resulting in significant health challenges. Additionally, LSS has been implicated in the regulation of cellular cholesterol levels and membrane integrity, making it a target for therapeutic interventions. The recombinant expression of LSS in various systems allows for detailed characterization of its enzymatic properties, substrate specificity, and the effects of various inhibitors or mutations. Understanding LSS's structure-function relationships through recombinant protein studies provides insights into lipid metabolism and potential pathways to manipulate these processes for clinical benefits, such as developing new treatments for hypercholesterolemia and other lipid-related disorders. Furthermore, as researchers explore the interplay between LSS and other metabolic enzymes, the findings may contribute to a more comprehensive understanding of the intricate networks governing lipid homeostasis in human health and disease. Overall, investigations into LSS as a recombinant protein represent a promising avenue for advancing both basic science and potential therapeutic strategies.
