关键信息
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基因名
FAHD1
- 应用
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别名
Acylpyruvase FAHD1; C16orf36; Chromosome 16 open reading frame 36; DKFZP566J2046; FAHD1; FAHD1_HUMAN; Fumarylacetoacetate hydrolase domain containing protein 1; Fumarylacetoacetate hydrolase domain-containing protein 1; MGC74876; mitochondrial; YISK like; YISK like/RJD15; YisK-like protein; YISKL
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q6P587
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表达区间
1-47aa
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氨基酸序列
MFQITFRCLPNFLRFGHHQEAFVKIKISTNYWPISDLLNQFDRINLQ
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分子量
32.1 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.
质检流程
相关产品
背景信息
FAHD1, or fatty acid hydrolase domain-containing protein 1, has emerged as a significant focus of research due to its potential role in various biological processes and its implications in metabolic disorders. Initially identified through genomic studies, FAHD1 is presumed to be involved in fatty acid metabolism, influencing energy homeostasis and lipid storage. Various studies have suggested that dysregulation of FAHD1 expression may correlate with conditions such as obesity, diabetes, and cardiovascular diseases. The protein’s unique structure, characterized by a hydrolase domain, enables it to interact with various substrates, making it a potential target for therapeutic interventions. Recent advances in recombinant protein technology have facilitated the expression and purification of FAHD1, allowing researchers to explore its enzymatic properties and functional roles in greater detail. Furthermore, understanding the molecular mechanisms governing FAHD1 activity could pave the way for novel strategies in managing metabolic disorders. As research progresses, FAHD1 is positioned as a promising candidate for further investigation within the scope of metabolic health and disease prevention, highlighting the need for comprehensive studies to elucidate its physiological significance and potential applications in biomedical science.
