Analytical Data
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基因名
ATP6AP2
- Application
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别名
ATP6AP2；Renin
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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
O75787
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表达区间
17-350aa
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氨基酸序列
NEFSILKSPGSVVFRNGNWPIPGERIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATVMVMVKGVNKLALPPGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLSSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDEIGKRYGEDSEQFRDASKILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLIRKTRTILEAKQAKNPASPYNLAYKYNFEYSVVFNMVLWIMIALALAVIITSYNIWNMDPGYDSIIYRMTNQKIRMD
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分子量
41.5 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
ATP6AP2, also known as ATPase H+ transporting accessory protein 2, is a crucial component implicated in various biological processes, including pH regulation and cellular signaling. Recent studies have highlighted its role in modulating the activity of V-ATPases (vacuolar ATPases), which are essential for maintaining intracellular pH and facilitating protein sorting in cells. Aberrations in ATP6AP2 expression have been linked to several diseases, including cancer and neurodevelopmental disorders, making it a significant target for therapeutic intervention. The recombinant expression of ATP6AP2 allows for the comprehensive analysis of its structure-function relationships and its interactions with other proteins, further elucidating its role in cellular mechanisms. Understanding the biochemical properties and regulatory mechanisms of ATP6AP2 is vital for developing targeted treatments and advancing our understanding of its relevance in health and disease. As a result, the research into ATP6AP2 recombinants is not only of academic interest but also holds promise for practical applications in medicine and biotechnology, paving the way for novel therapeutic strategies.
