Analytical Data
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Gene name
YUAB
- Application
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Alternative Names
ORF-1
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Species
strain 168
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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
P71014
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Expression Region
1-181aa
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Molecular Weight
35.3 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
The study of YUAB recombinant proteins has emerged at the forefront of biotechnology and protein engineering due to their potential applications in various fields such as medicine, agriculture, and environmental science. YUAB proteins, derived from specific biological organisms, are designed to be expressed in host systems, enabling scientists to harness their unique functional properties. The significance of YUAB recombinant proteins lies in their ability to undergo post-translational modifications, which can enhance their stability, activity, and specificity. Research in this area aims to optimize the expression systems and purification processes to produce large quantities of high-quality proteins. Additionally, understanding the structure-function relationships of YUAB proteins is crucial for developing therapeutic agents, vaccines, and bioactive compounds that can address pressing health challenges and improve food security. The ongoing advances in molecular biology, including CRISPR technology and advanced computational modeling, have accelerated the research and development of YUAB recombinant proteins, paving the way for innovative solutions that could revolutionize various industries. Consequently, the exploration of YUAB protein characteristics and their potential functionalities remains a robust area of investigation, promising to unlock new avenues for scientific discovery and practical applications.
