Analytical Data
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Gene name
iceE
- Application
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Alternative Names
Ice nucleation protein
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Species
Enterobacter agglomerans
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P16239
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Expression Region
1129-1258aa
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Molecular Weight
15.7 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 iceE recombinant protein originates from the need to understand and manipulate the mechanisms of protein expression in extreme environments. IceE, a gene derived from psychrophilic organisms, has been shown to play a crucial role in cold adaptation, allowing these microorganisms to thrive at low temperatures. Researchers are particularly interested in the iceE gene due to its potential applications in biotechnology and industrial processes, where cold-active enzymes can enhance efficiency and reduce energy costs. The expression and characterization of IceE recombinant protein provide insights into its structural and functional properties, which can be leveraged for the development of innovative biocatalysts. Additionally, understanding the evolutionary adaptations that enable psychrophiles to function in frigid conditions offers valuable information that can inspire advances in enzyme engineering and cold-process biomanufacturing. The research contributes to a broader understanding of protein adaptations to environmental extremes, which is relevant not only to biotechnology but also to ecological and evolutionary studies.
