Analytical Data
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Gene name
SPE39
- Application
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Alternative Names
VPS33B-interacting protein in apical-basolateral polarity regulatorVPS33B-interacting protein in polarity and apical restriction
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Species
Human
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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
Q9H9C1
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Expression Region
1-493aa
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Molecular Weight
73 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
SPE39, or Sphingomonas sp. strain E-39 protein, has garnered significant interest in the field of molecular biology due to its unique enzymatic properties and potential biotechnological applications. Originally identified in the metabolically versatile bacterium Sphingomonas, SPE39 is notable for its ability to degrade complex environmental pollutants, including aromatic compounds, making it a candidate for bioremediation efforts. Its role in microbial metabolism highlights the significance of such proteins in ecological processes and pollution management. Researchers focus on the recombinant expression of SPE39 to elucidate its structure-function relationships and enzymatic mechanisms. Through techniques like cloning, expression in heterologous systems, and biochemical characterization, scientists aim to enhance its stability and activity for practical applications. Additionally, understanding the evolutionary adaptations of SPE39 can foster the development of engineered variants with improved performance in industrial processes. The exploration of SPE39 not only contributes to our fundamental knowledge of microbial ecology and enzymology but also paves the way for innovative solutions to environmental challenges.
