Analytical Data
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Gene name
iceE
- Application
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Alternative Names
iceE；Caspase-14
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
MAGERGKLIAGADSTQTAGDRSKLLAGNNSYLTAGDRSKLTAGNDCILMAGDRSKLTAGINSILTAGCRSKLIGSNGSTLTAGENSVLIFRCWDGKRYTNVVAKTGKGGIEADMPYQMDEDNNIVNKPEE
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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 proteins is rooted in the understanding of the molecular mechanisms of antifreeze proteins, which play a critical role in the survival of various organisms in cold environments. IceE, derived from polar bacteria, has been shown to possess remarkable ice-binding properties that prevent ice crystal formation and promote supercooling. This characteristic is of significant interest for applications in food preservation, biotechnology, and materials science. Researchers aim to explore the structural and functional aspects of iceE, particularly its ability to inhibit ice crystal growth, which could lead to innovations in cryopreservation techniques and the development of new antifreeze agents. By employing recombinant DNA technology, scientists are able to produce iceE in a more controlled and scalable manner, allowing for detailed studies of its properties and potential applications. Given the increasing demands for sustainable solutions in cold-chain logistics and food safety, understanding and harnessing the capabilities of iceE recombinant proteins could contribute to advancements in multiple fields, including agriculture, medicine, and environmental science. This research not only enhances our fundamental knowledge of protein behavior in extreme conditions but also paves the way for practical applications that address real-world challenges related to temperature-dependent processes.
