Analytical Data
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基因名
HEATR6
- Application
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别名
HEATR6；ABC1；HEAT repeat-containing Protein 6
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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
Q6AI08
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表达区间
1052-1175aa
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氨基酸序列
KSEDTIDFLEFKYCVSLRTQICQALIHLLSLASASDLPCMKETLELSGNMVQSYILQFLKSGAEGDDTGAPHSPQERDQMVRMALKHMGSIQAPTGDTARRAIMGFLEEILAVCFDSSGSQGAL
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分子量
18.5 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
HEATR6, a member of the HEAT repeat-containing protein family, has garnered significant interest in recent years due to its potential roles in cellular processes, such as chromatin remodeling and RNA metabolism. The HEAT repeats, structural motifs characterized by the presence of alternating alpha-helices and loops, contribute to the stability and functionality of proteins involved in critical cellular pathways. Research has indicated that HEATR6 may be involved in the regulation of gene expression and the maintenance of genome integrity. Its association with various human diseases, including cancer, highlights the necessity of understanding its biochemical properties and interactions. Effective study of HEATR6 requires the production of recombinant protein, allowing researchers to explore its structure-function relationships in vitro. The purification and characterization of HEATR6 as a recombinant protein can facilitate the investigation of its binding partners and functional mechanisms. Additionally, insights into its role in cellular response to stress and its involvement in signal transduction pathways may provide valuable information for therapeutic strategies targeting diseases related to HEATR6 dysregulation. Therefore, the ongoing research into HEATR6 recombinant protein is critical for elucidating the multifaceted roles of this protein in human health and disease.
