Analytical Data
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基因名
cia
- Application
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别名
cia；CIA1；WDR39；Probable cytosolic iron-sulfur Protein assembly Protein CIAO1
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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
P06716
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表达区间
1-626aa
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氨基酸序列
MSDPVRITNPGAESLGYDSDGHEIMAVDIYVNPPRVDVFHGTPPAWSSFGNKTIWGGNEWVDDSPTRSDIEKRDKEITAYKNTLSAQQKENENKRTEAGKRLSAAIAAREKDENTLKTLRAGNADAADITRQEFRLLQAELREYGFRTEIAGYDALRLHTESRMLFADADSLRISPREARSLIEQAEKRQKDAQNADKKAADMLAEYERRKGILDTRLSELEKNGGAALAVLDAQQARLLGQQTRNDRAISEARNKLSSVTESLNTARNALTRAEQQLTQQKNTPDGKTIVSPEKFPGRSSTNHSIVVSGDPRFAGTIKITTSAVIDNRANLNYLLSHSGLDYKRNILNDRNPVVTEDVEGDKKIYNAEVAEWDKLRQRLLDARNKITSAESAVNSARNNLSARTNEQKHANDALNALLKEKENIRNQLSGINQKIAEEKRKQDELKATKDAINFTTEFLKSVSEKYGAKAEQLAREMAGQAKGKKIRNVEEALKTYEKYRADINKKINAKDRAAIAAALESVKLSDISSNLNRFSRGLGYAGKFTSLADWITEFGKAVRTENWRPLFVKTETIIAGNAATALVALVFSILTGSALGIIGYGLLMAVTGALIDESLVEKANKFWGI
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分子量
76.3 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
The research on CIA (Cysteine-Dependent Iron-Sulfur Cluster Assembly) protein focuses on understanding the molecular mechanisms by which cells assemble iron-sulfur (Fe-S) clusters, essential cofactors for various cellular processes. These clusters play crucial roles in electron transport, enzymatic activity, and regulation of gene expression. Disruption in CIA proteins can lead to diverse diseases, including neurodegenerative disorders and cancer, due to the impairment of mitochondrial function and oxidative stress. The complexity of CIA involves multiple protein components and intricate pathways that are still not fully elucidated. Recent advancements in structural biology and biochemistry have shed light on the assembly process and the interaction of CIA proteins with other cellular partners. This research is significant as it not only contributes to our understanding of fundamental biological processes but also opens avenues for therapeutic interventions targeting CIA pathways to mitigate the effects of diseases associated with Fe-S cluster dysfunction. By unraveling the intricacies of CIA protein mechanisms, scientists aim to develop strategies to enhance cellular resilience against oxidative damage and improve mitochondrial health, thereby offering potential benefits in various medical fields.
