Analytical Data
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Gene name
RPLP1
- Application
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Alternative Names
RPLP1；RRP1；Large ribosomal subunit Protein P1
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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
P05386
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Expression Region
2-114aa
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AA Sequence
ASVSELACIYSALILHDDEVTVTEDKINALIKAAGVNVEPFWPGLFAKALANVNIGSLICNVGAGGPAPAAGAAPAGGPAPSTAAAPAEEKKVEAKKEESEESDDDMGFGLFD
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Molecular Weight
27.4 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
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Protein Description
RPLP1, or Ribosomal Protein Lateral Stalk Subunit P1, is a crucial component of the ribosome, playing an essential role in protein synthesis and cellular function. Recent studies have highlighted its involvement in various cellular processes, including the regulation of translation, response to stress, and the maintenance of ribosomal integrity. Aberrations in RPLP1 expression have been linked to a range of diseases, particularly cancers, where its overexpression can contribute to enhanced protein synthesis and tumorigenesis. As a result, RPLP1 has attracted attention as a potential biomarker and therapeutic target. Researchers are now focused on the recombinant production of RPLP1 to facilitate detailed studies of its structure, function, and interactions with other cellular components. The ability to obtain RPLP1 in a pure and active form through recombinant techniques enables in vitro assays that investigate its role in ribosomal assembly and translational dynamics. This research may provide valuable insights into the molecular mechanisms underlying ribosome function and the pathological conditions associated with RPLP1 dysregulation, paving the way for innovative therapeutic strategies targeting its pathways in diseases such as cancer. Overall, the recombinant RPLP1 protein serves as a powerful tool for exploring the intricacies of ribosomal biology and its implications in health and disease.
