Analytical Data
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Gene name
Serum Albumin
- Application
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Alternative Names
Albumin; Alb
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Species
Rat
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Source
HEK293
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Tag
N-8*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P02770
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Expression Region
E25-A608
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Protein Length
Full Length of Mature Protein
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Molecular Weight
Predicted band size: 67.52 kDa; Observed band size: 65-70 kDa.
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
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.
