Analytical Data
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Gene name
E54K,L372P
- Application
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Alternative Names
Transposase for transposon Tn5(EC 3.1.-.-)(Tnp)
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Species
Escherichia coli
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q46731
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Expression Region
1-476aa(E54K,L372P)
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Molecular Weight
53.4 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 E54K and L372P variants of recombinant protein have garnered significant attention in recent years due to their potential implications in various biological and medical fields. These mutations are often explored in the context of protein structure-function relationships, particularly in regard to their stability and interaction with other biomolecules. The E54K substitution, which involves a conservative replacement of a glutamic acid residue with lysine, can influence the protein's charge distribution and hydrophobicity, potentially enhancing its stability under certain conditions. Conversely, the L372P mutation introduces a proline residue that can disrupt local secondary structures, leading to altered dynamics and folding properties. Understanding the molecular mechanisms by which these mutations affect the protein's behavior is crucial for elucidating their biological roles and potential therapeutic applications. In the realm of disease research, such as in cancer or metabolic disorders, these variants may serve as biomarkers or therapeutic targets, thus highlighting the importance of studying their structural and functional implications. Experimental approaches, including X-ray crystallography, NMR spectroscopy, and computational modeling, are employed to characterize these proteins, shedding light on how specific mutations can either contribute to or mitigate disease processes. Furthermore, optimizing the expression and purification protocols of these recombinant proteins enhances their utility in both basic research and clinical applications, underlining the significance of these studies in advancing our understanding of protein engineering and disease mechanisms. Overall, the investigation of E54K and L372P variants is a vital area of research with broad implications in biochemistry, molecular biology, and therapeutic development.
