Analytical Data
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基因名
Lipoate-protein ligase A/LplA
- Application
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别名
Lipoate--protein ligase
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种属
Escherichia coli
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
C4ZT68
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表达区间
1-338aa
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分子量
53.9 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
Lipoate-protein ligase A (LplA) plays a crucial role in the post-translational modification of proteins by catalyzing the attachment of lipoate, a bioactive lipid cofactor, to specific lysine residues on target proteins. This modification is essential for the proper functioning of several key enzymes involved in mitochondrial metabolism, including those in the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes. Given its significance, LplA has garnered attention in the field of biochemistry and molecular biology, with researchers investigating its structure, mechanism, and potential applications. The ability to produce recombinant LplA in sufficient quantities allows for detailed functional studies and the development of assays to screen for inhibitors that could modulate its activity, thereby providing insights into metabolic diseases associated with dysfunctional lipoic acid metabolism. Additionally, understanding LplA has implications for biotechnology, particularly in the development of novel therapeutics that exploit lipoate attachment for enhancing protein function or stability. Overall, the study of LplA not only illuminates fundamental biological processes but also opens avenues for innovative solutions in medicine and industry.
