Analytical Data
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基因名
Serum Albumin
- Application
-
别名
Albumin; Alb
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种属
Rat
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表达系统
HEK293
-
标签
N-8*His
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P02770
-
表达区间
E25-A608
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蛋白长度
Full Length of Mature Protein
-
分子量
Predicted band size: 67.52 kDa; Observed band size: 65-70 kDa.
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
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.
-
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.
-
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
Serum albumin, a vital blood protein synthesized primarily in the liver, plays a crucial role in maintaining oncotic pressure, transporting various substances, and regulating blood volume. Due to its significant physiological functions and abundance in plasma, recombinant human serum albumin (rHSA) has garnered significant attention in biomedical research and clinical applications. The development of rHSA has emerged as a promising alternative to human serum albumin sourced from blood donors, mitigating risks of transmission of infectious agents and providing a sustainable supply for therapeutic uses. Moreover, rHSA can be engineered for enhanced properties, such as increased stability and improved binding affinity for drugs and other molecules, thereby expanding its application in drug delivery, as a stabilizing agent in biopharmaceutical formulations, and in various clinical settings requiring volume expansion or protein supplementation. Recent advances in recombinant DNA technology facilitate the production of rHSA with high purity and yield, rendering it increasingly viable for widespread therapeutic use. Furthermore, ongoing research aims to better understand its interactions within the body and its potential modifications to optimize its efficacy and safety profiles in diverse medical applications. This background underscores the significance of rHSA research in addressing both clinical needs and improving patient outcomes, making it a focal point of contemporary biomedical studies.












