Analytical Data
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Gene name
speF
- Application
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Alternative Names
speF; b0693; JW0680; Inducible ornithine decarboxylase; EC 4.1.1.17
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Species
Escherichia coli
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Source
E. coli
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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
P24169
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Expression Region
1-732aa
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Molecular Weight
86.4 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 study of speF recombinant protein has garnered significant interest due to its crucial role in the biosynthesis of polyamines, which are essential for various cellular processes, including cell growth, differentiation, and proliferation. SpeF, or S-adenosylmethionine decarboxylase, is an enzyme that catalyzes the decarboxylation of S-adenosylmethionine (SAM) to produce decarboxylated SAM, the precursor for polyamine synthesis. Abnormal regulation of polyamine levels has been linked to numerous diseases, including cancer, making the understanding of SpeF and its function increasingly important. Researchers are focusing on the recombinant expression of SpeF to investigate its biochemical properties, structural characteristics, and the implications of its activity in polyamine metabolism. By producing SpeF in a controlled environment, scientists aim to determine its enzymatic kinetics and the effect of various substrates and inhibitors, thereby shedding light on its underlying mechanisms. Moreover, the use of recombinant techniques allows for the incorporation of modifications that could enhance its stability and activity, potentially leading to therapeutic applications. Overall, the exploration of speF recombinant protein not only contributes to a detailed understanding of polyamine biosynthesis but also holds promise for developing strategies to combat diseases associated with polyamine dysregulation.
