Analytical Data
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Gene name
RPL18
- Application
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Alternative Names
RPL18；Large ribosomal subunit Protein eL18
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Species
Human
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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
Q07020
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Expression Region
2-187aa
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AA Sequence
GVDIRHNKDRKVRRKEPKSQDIYLRLLVKLYRFLARRTNSTFNQVVLKRLFMSRTNRPPLSLSRMIRKMKLPGRENKTAVVVGTITDDVRVQEVPKLKVCALRVTSRARSRILRAGGKILTFDQLALDSPKGCGTVLLSGPRKGREVYRHFGKAPGTPHSHTKPYVRSKGRKFERARGRRASRGYK
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Molecular Weight
48.4 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
RPL18 is a crucial component of the ribosomal protein family, playing an integral role in the ribosome's function, which is essential for protein synthesis in all living organisms. Recent studies have highlighted its involvement in various cellular processes, including cell growth, differentiation, and response to stress. The aberrant expression of RPL18 has been linked to several diseases, including cancer, where it may exhibit oncogenic properties by influencing the translation of specific mRNAs related to cell proliferation and survival. Advances in recombinant protein technology have facilitated the production of RPL18 in a heterologous expression system, allowing for detailed functional analyses and structural studies. Understanding the molecular mechanisms by which RPL18 operates can provide insights into its role in ribosome biogenesis and its potential as a therapeutic target. This research is pivotal, not only for basic biological understanding but also for its implications in developing strategies to combat diseases associated with ribosomal dysfunctions, marking RPL18 as a significant focus within molecular biology and biomedical research.
