Analytical Data
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基因名
AQP1
- Application
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别名
Aquaporin-CHIP Urine water channel Water channel protein for red blood cells and kidney proximal tubule
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种属
Human
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P29972
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表达区间
2-269aa
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分子量
41.3kDa
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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
Aquaporin-1 (AQP1) is a water channel protein that plays a crucial role in water transport across cell membranes. It is predominantly expressed in kidney and erythrocyte cells, facilitating osmotic water flow and contributing to the regulation of body water homeostasis. Research into AQP1 has gained momentum due to its significant implications in various physiological and pathological conditions, including kidney function, brain edema, and cancer progression. The study of AQP1 and its recombinant forms allows for a deeper understanding of its structure-function relationship and its role in membrane biology. Recombinant AQP1 proteins can be produced in various systems, enabling the investigation of their biophysical properties, gating mechanisms, and interactions with other cellular components. Furthermore, AQP1 is also being explored as a potential therapeutic target for diseases characterized by dysregulated water transport, making its study increasingly relevant. By elucidating the molecular mechanisms underlying AQP1 function, researchers aim to identify novel strategies for clinical interventions, thereby advancing our knowledge in both basic and applied biomedical sciences.
