Analytical Data
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Gene name
RPLP0
- Application
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Alternative Names
Rplp0; Arbp; 60S acidic ribosomal protein P0; 60S ribosomal protein L10E
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Species
Mouse
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Source
E. coli
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Tag
N-10*His;C-Myc;N-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P14869
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Expression Region
M1-D317
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Protein Length
Full Length
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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
RPLP0, or Ribosomal Protein Lateral Stalk Subunit P0, is a critical component of the ribosomal stalk structure, which plays a fundamental role in protein synthesis in eukaryotic cells. This protein is part of the large ribosomal subunit and is involved in the interactions between the ribosome and various factors during translation, influencing the overall efficiency and regulation of protein synthesis. Research into RPLP0 has gained importance due to its implications in cell growth and proliferation, as well as its potential involvement in cancer biology. Alterations or mutations in ribosomal proteins, including RPLP0, have been linked to various diseases, particularly malignancies, where disruptions in protein synthesis can lead to uncontrolled cell division. Consequently, the study of RPLP0 as a recombinant protein has emerged as a significant area for understanding its structure-function relationship and regulatory mechanisms in ribosomal activity. Furthermore, recombinant RPLP0 can serve as a valuable tool in structural biology and biochemistry, allowing for detailed studies on ribosomal dynamics and the development of therapeutic strategies targeting ribosome-associated pathways. Insights from RPLP0 research may pave the way for novel approaches in cancer treatment and provide a deeper understanding of the fundamental processes of life at the molecular level.
