Analytical Data
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基因名
ILVBL
- Application
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别名
ILVBL；AHAS；HACL2；2-hydroxyacyl-CoA lyase 2
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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
A1L0T0
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表达区间
1-632aa
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氨基酸序列
METPAAAAPAGSLFPSFLLLACGTLVAALLGAAHRLGLFYQLLHKVDKASVRHGGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVLYPYFMVQKEMVPAKPPKGLVGRVVSWYLENYLANLFAGAWEPQPEGPLPLDIPQASPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRSAALKKADVIVLAGTVCDFRLSYGRVLSHSSKIIIVNRNREEMLLNSDIFWKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVEELREADRQKEQTFREKAAMPVAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACGLAYTDYHKAAMGLGARGLLLSRENEDQVVKVLHDAQQQCRDGHPVVVNILIGRTDFRDGSIAV
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分子量
67.8 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, or isovaleryl-CoA dehydrogenase, is a key enzyme involved in the catabolism of branched-chain amino acids, particularly leucine, isoleucine, and valine. Its importance lies in its role in the mitochondrial pathway for the degradation of these amino acids, which are crucial for energy production and metabolic regulation. Mutations in the ILVBL gene have been linked to various metabolic disorders, leading to an accumulation of toxic metabolites and contributing to serious health issues, including metabolic crises in affected individuals. Given the rising prevalence of metabolic diseases worldwide, understanding ILVBL's structure, function, and interaction with other metabolic pathways has become increasingly important. Recent advancements in recombinant protein technology have enabled the production and purification of ILVBL in sufficient quantities for detailed biochemical studies. This allows researchers to investigate its enzymatic mechanisms, substrate specificity, and potential regulatory roles within the metabolic network. Moreover, such studies may also facilitate the development of targeted therapies for enzymatic deficiencies arising from ILVBL dysfunction. By elucidating the functional aspects of ILVBL through reconstituted protein studies, scientists aim to gain insights that could contribute to better diagnostic tools and therapeutic strategies for managing metabolic disorders associated with branched-chain amino acid metabolism. Thus, the research on ILVBL recombinant protein is not only significant for basic biochemical understanding but also holds promise for translational applications in medicine.
