Analytical Data
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基因名
REN
- Application
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别名
REN;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
P00797
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表达区间
1-406aa
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氨基酸序列
MDGWRRMPRWGLLLLLWGSCTFGLPTDTTTFKRIFLKRMPSIRESLKERGVDMARLGPEWSQPMKRLTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR
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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
REN (Renin) is a key enzyme in the renin-angiotensin-aldosterone system (RAAS), which plays a crucial role in regulating blood pressure, fluid balance, and electrolyte homeostasis. Research on REN has gained significant attention due to its implications in various cardiovascular and renal diseases, including hypertension, heart failure, and chronic kidney disease. Abnormal REN activity can lead to pathological conditions, making it a potential therapeutic target. Advances in recombinant protein technology have enabled the production of recombinant REN, facilitating the study of its structure, function, and interactions with various inhibitors. This not only enhances our understanding of REN's role in disease but also aids in the development of novel pharmacological interventions. Furthermore, the investigation of REN's mechanisms in cellular signaling and tissue responses provides insights into its broader physiological effects. Overall, the study of REN and its recombinant forms is pivotal for developing innovative strategies to combat cardiovascular and renal disorders, highlighting the importance of ongoing research in this field.
