Analytical Data
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Gene name
RPL5
- Application
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Alternative Names
RPL5;Large ribosomal subunit Protein uL18
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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
P46777
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Expression Region
1-297aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMGFVKVVKNKAYFKRYQVKFRRRREGK TDYYARKRLVIQDKNKYNTPKYRMIVRVTNRDIICQIAYARIEGDMIVCA AYAHELPKYGVKVGLTNYAAAYCTGLLLARRLLNRFGMDKIYEGQVEVTG DEYNVESIDGQPGAFTCYLDAGLARTTTGNKVFGALKGAVDGGLSIPHST KRFPGYDSESKEFNAEVHRKHIMGQNVADYMRYLMEEDEDAYKKQFSQYI KNSVTPDMMEEMYKKAHAAIRENPVYEKKPKKEVKKKRWNRPKMSLAQKK DRVAQKKASFLRAQERAAES
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Molecular Weight
37 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
RPL5, a ribosomal protein that is a component of the large subunit of ribosomes, plays a crucial role in ribosome biogenesis and protein synthesis. It is encoded by the RPL5 gene located on human chromosome 1 and is implicated in various cellular processes. Recent studies have highlighted the significance of RPL5 in cellular stress responses, particularly its involvement in the p53 pathway, where it acts as a regulator of ribosome assembly and function. Abnormalities in RPL5 expression have been linked to several forms of cancer and genetic disorders such as Diamond-Blackfan anemia, underscoring its importance in maintaining cellular homeostasis and proper ribosome function. The recombinant expression of RPL5 allows for a detailed analysis of its molecular structure and interactions, aiding in the understanding of its functional mechanisms within the ribosome and its role in disease. Utilizing recombinant techniques, researchers aim to produce purified RPL5 protein for biochemical assays and crystallography studies, which will provide insights into its structure-function relationship and its implications in pathology. Understanding RPL5's reconstitution and functional dynamics can potentially lead to novel therapeutic strategies in cancer treatment and the modulation of ribosome-related diseases. Consequently, the study of RPL5 as a recombinant protein not only enriches our understanding of ribosome biology but also opens avenues for future biomedical applications.
