Analytical Data
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Gene name
RPL11
- Application
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Alternative Names
RPL11;Large ribosomal subunit Protein uL5
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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
P62913
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Expression Region
1-178aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAQDQGE KENPMRELRI RKLCLNICVG ESGDRLTRAA KVLEQLTGQT PVFSKARYTV RSFGIRRNEK IAVHCTVRGA KAEEILEKGL KVREYELRKN NFSDTGNFGF GIQEHIDLGI KYDPSIGIYG LDFYVVLGRP GFSIADKKRR TGCIGAKHRI SKEEAMRWFQ QKYDGIILPG K
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Molecular Weight
23 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
RPL11, a crucial ribosomal protein, is a component of the 60S ribosomal subunit and plays a significant role in ribosome biogenesis and protein synthesis. Recent studies have highlighted its involvement in various cellular processes beyond its traditional function in translation, including cell cycle regulation and tumor suppression. RPL11 has been discovered to interact with key regulatory pathways, such as the p53 tumor suppressor pathway, emphasizing its potential role in cellular stress responses and the maintenance of genomic integrity. Alterations in RPL11 expression or function have been linked to various cancers, suggesting that it may serve as a biomarker for tumor progression or as a candidate for targeted therapies. Furthermore, research into RPL11's structural dynamics and reassembly mechanisms underlines its importance in maintaining ribosomal integrity and functionality. As researchers continue to explore the multifaceted roles of RPL11 in both normal physiology and disease states, its potential as a therapeutic target and its involvement in the pathogenesis of various malignancies make it a significant focus of contemporary biomedical research.
