Analytical Data
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Gene name
RPL28
- Application
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Alternative Names
RPL28；Large ribosomal subunit Protein eL28
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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
P46779
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Expression Region
2-137aa
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AA Sequence
SAHLQWMVVRNCSSFLIKRNKQTYSTEPNNLKARNSFRYNGLIHRKTVGVEPAADGKGVVVVIKRRSGQRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMAAIRRASAILRSQKPVMVKRKRTRPTKSS
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Molecular Weight
42.6 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
RPL28, a critical component of the ribosomal subunit, plays a significant role in the assembly and function of the ribosome, the cellular machinery responsible for protein synthesis. Research into RPL28 often focuses on its involvement in ribosome biogenesis, as well as its importance in cellular growth and proliferation. Abnormalities in RPL28 expression or function have been implicated in various diseases, including cancer, where dysregulated protein synthesis is a hallmark. Additionally, RPL28 is subject to post-translational modifications that may influence its interaction with other ribosomal proteins and RNA, thereby affecting ribosome stability and translational accuracy. Recent studies have employed recombinant DNA technology to express and purify RPL28, allowing for detailed investigations into its structural properties and interactions with other ribosomal components. This research is essential not only for understanding the fundamental mechanisms of protein synthesis but also for exploring potential therapeutic interventions targeting ribosomal dysfunctions in diseases. Furthermore, advances in techniques such as cryo-electron microscopy have provided insights into the structural organization of ribosomes and the specific role of RPL28, offering new avenues for research in ribosomal biology and its implications for health and disease.
