Analytical Data
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基因名
ILVBL
- Application
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别名
IlvB-like protein
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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
A1L0T0
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表达区间
1-632aa
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分子量
70.7 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
ILVBL (isovaleryl-CoA dehydrogenase-like protein) is a member of the acyl-CoA dehydrogenase family, which plays a crucial role in the mitochondrial fatty acid oxidation and branched-chain amino acid metabolism. The importance of ILVBL arises from its involvement in various metabolic pathways essential for energy production and metabolic homeostasis. Mutations or dysfunction in ILVBL have been linked to metabolic disorders, which can result in significant health issues, including energy metabolism impairments and neurological symptoms. Understanding the structure and function of ILVBL is vital for elucidating its role in these metabolic pathways and may lead to potential therapeutic targets for conditions associated with its dysregulation. Recent advances in recombinant technology have enabled the expression and purification of ILVBL protein, facilitating in-depth biochemical and structural studies. These investigations aim to shed light on its enzymatic mechanisms and regulation, paving the way for novel insights into metabolic diseases and potential interventions. By exploring the functional dynamics of ILVBL, researchers hope to contribute to the understanding of metabolic pathways and develop strategies to counteract the effects of metabolic disorders.
