Analytical Data
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Gene name
albA
- Application
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Alternative Names
albA; PF1881DNA/RNA-binding protein Alba
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Species
Pyrococcus furiosus
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8TZV1
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Expression Region
1-93aa
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Molecular Weight
26.4 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
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Protein Description
AlbA, an albumin-binding protein, has garnered significant attention in the field of biomedical research due to its unique properties and potential applications. Initially discovered in *Bacillus subtilis*, AlbA is known for its ability to bind to human serum albumin, a prevalent protein in the bloodstream with numerous physiological roles. Studies have revealed that AlbA can enhance the solubility and stability of various therapeutic proteins, making it a valuable tool in drug delivery systems. Researchers are particularly interested in its role in improving the pharmacokinetics of drugs, allowing for prolonged circulation time and reduced dosage frequency, which can lead to improved patient compliance and therapeutic outcomes. Moreover, the engineering of AlbA for targeted drug delivery holds promise in oncological applications, where localized therapy is crucial for minimizing side effects. The exploration of AlbA’s structure-function relationship also provides insights into protein-protein interactions that are fundamental to many biological processes. Recent advances in recombinant DNA technology have enabled the production of AlbA in various host systems, facilitating extensive studies into its functionality and interaction mechanisms. Overall, the ongoing research on AlbA not only contributes to the understanding of protein behavior in biological systems but also paves the way for innovative strategies in drug formulation and delivery, with the potential to transform treatment paradigms for various diseases.
