Analytical Data
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Gene name
RPLP1
- Application
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Alternative Names
P1; RPP1
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Species
Human
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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
P05386
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Expression Region
Ala2~Asp114
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Molecular Weight
19kDa
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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
RPLP1, or Ribosomal Protein Lateral Stalk Subunit P1, is a critical component of the ribosomal stalk in eukaryotic ribosomes, playing a vital role in translation and ribosomal function. Its structure and functionality are essential for ribosome interaction with factors involved in protein synthesis, including elongation factors and GTPases. Research into RPLP1 has gained significance due to its implications in various cellular processes and diseases, including cancer, where altered ribosomal function is often observed. Moreover, RPLP1 contributes to the overall translation fidelity and efficiency, making it a potential target for therapeutic interventions. The study of recombinant RPLP1 proteins has facilitated insights into their structural properties, binding mechanisms, and interaction domains, contributing to a deeper understanding of ribosomal assembly and function. By exploring the role of RPLP1 within the context of ribosome dynamics, researchers aim to elucidate how disturbances in this protein can lead to pathological states, bridging the gap between basic biological research and clinical applications. Overall, the investigation of RPLP1 and its recombinant forms holds promise for advancing our knowledge of ribosomal biology and developing novel strategies to modulate protein synthesis in disease contexts.
