Analytical Data
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基因名
ECH1
- Application
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别名
HPXEL; Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial
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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 90% as determined by SDS-PAGE.
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蛋白编号
Q13011
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表达区间
Met1~Leu328
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分子量
40kDa
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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
ECH1 (enoyl-CoA hydratase 1) is an essential enzyme in the mitochondrial fatty acid β-oxidation pathway, playing a crucial role in the catabolism of medium- and long-chain fatty acids. Deficiencies in ECH1 have been linked to various metabolic disorders, including very-long-chain acyl-CoA dehydrogenase deficiency (VLCADD) and other fatty acid oxidation-related pathologies. The study of ECH1 recombinant protein is vital for further understanding its structure-function relationships and the underlying mechanisms of its activity. Recent advances in recombinant DNA technology have enabled the expression of ECH1 in heterologous systems, facilitating the purification and characterization of the protein. Researchers are particularly interested in elucidating the enzyme's kinetic properties, substrate specificity, and interaction with cofactors, which are crucial for its catalytic function. Additionally, investigating the impact of mutations on ECH1's activity could provide insights into the pathophysiology of related metabolic disorders. Such studies not only contribute to the fundamental knowledge of lipid metabolism but also have potential therapeutic implications, paving the way for the development of targeted treatments for conditions associated with ECH1 dysfunction. Overall, the research on ECH1 recombinant protein serves as a vital bridge connecting molecular biology and clinical applications, with the potential to improve diagnosis and treatment strategies for metabolic diseases.
