Analytical Data
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Gene name
rplF
- Application
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Alternative Names
rplF; b3305; JW3267; 50S ribosomal protein L6; Large ribosomal subunit protein uL6
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Species
Escherichia coli
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0AG55
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Expression Region
2-175aa
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Molecular Weight
45.5 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
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Protein Description
The RplF protein, a vital component of the ribosomal protein family, plays a crucial role in the assembly and function of the ribosome, which is essential for protein synthesis in all living organisms. Research on RplF is particularly significant due to its implications in understanding the mechanisms of translation and the regulation of gene expression. Moreover, alterations or mutations in ribosomal proteins like RplF have been linked to various diseases, including cancer. The study of RplF recombinant protein aims to delineate its structural and functional properties, enabling insights into how it interacts with ribosomal RNA and other proteins during ribosome assembly. By producing RplF in a recombinant form, researchers can conduct in-depth analyses, including crystallization studies, binding assays, and functional assays, to explore its role in translational regulation and cellular responses to stress. The findings from RplF research could shed light on the broader aspects of ribosome biology and provide potential therapeutic targets for diseases associated with ribosome dysfunction.
