Analytical Data
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Gene name
eco
- Application
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Alternative Names
eco；ICK；KIAA0936;Serine/threonine-Protein kinase ICK
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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
B7UFM3
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Expression Region
21-162aa
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AA Sequence
AESVQPLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLESKTLEGWGYDYYVFDKVSSPVSTMMACPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTPDNVDVKYRVWKAEEKIDNAVVR
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Molecular Weight
23.5 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 eco-recombinant proteins has gained significant attention due to their potential applications in biotechnology, medicine, and environmental sustainability. Eco-recombinant proteins are engineered proteins produced through recombinant DNA technology, allowing for the modification of amino acid sequences to enhance their functionality, stability, and specificity. This research is rooted in the necessity for efficient enzymes and proteins that can withstand extreme conditions, such as high temperatures or acidic environments, which are often encountered in industrial processes. Additionally, eco-recombinant proteins play a crucial role in developing biocatalysts for green chemistry, thereby reducing reliance on hazardous chemicals. The ability to produce these proteins in various host systems, including bacteria, yeast, and plants, has opened new avenues for research into their therapeutic potential, such as developing vaccines and therapeutic enzymes for disease treatment. Furthermore, the growing emphasis on sustainable practices has propelled interest in eco-recombinant proteins that can be utilized in bioremediation efforts to address environmental contamination. As a result, multidisciplinary approaches combining molecular biology, protein engineering, and environmental science are being employed in this field, driving innovation and facilitating the discovery of novel proteins with desirable characteristics for a myriad of applications. The ongoing advancements in techniques such as CRISPR and synthetic biology are expected to further accelerate research in eco-recombinant proteins, heralding a new era of biotechnological breakthroughs.
