Analytical Data
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Gene name
RPL8
- Application
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Alternative Names
RPL8;Large ribosomal subunit Protein uL2
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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
P62917
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Expression Region
1-257aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGRVIRGQRK GAGSVFRAHV KHRKGAARLR AVDFAERHGY IKGIVKDIIH DPGRGAPLAK VVFRDPYRFK KRTELFIAAE GIHTGQFVYC GKKAQLNIGN VLPVGTMPEG TIVCCLEEKP GDRGKLARAS GNYATVISHN PETKKTRVKL PSGSKKVISS ANRAVVGVVA GGGRIDKPIL KAGRAYHKYK AKRNCWPRVR GVAMNPVEHP FGGGNHQHIG KPSTIRRDAP AGRKVGLIAA RRTGRLRGTK TVQEKEN
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Molecular Weight
30 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
RPL8, a ribosomal protein component of the 60S subunit, plays a pivotal role in the synthesis of proteins within eukaryotic cells. Recent studies have highlighted its involvement not only in ribosome biogenesis but also in various cellular processes, including cell proliferation and stress responses. Abnormal expression of RPL8 has been linked to several diseases, such as cancer, where it contributes to the dysregulation of the cellular machinery that controls growth and division. As researchers continue to investigate the multifaceted roles of ribosomal proteins like RPL8, they are exploring its potential as a biomarker for disease progression and as a target for therapeutic intervention. Understanding the structural and functional properties of RPL8 through recombinant protein studies can offer insights into its mechanistic functions and interactions with other cellular components. Moreover, advancements in techniques such as CRISPR-Cas9 gene editing and high-throughput sequencing are facilitating deeper investigations into RPL8's role in various biological contexts, highlighting its significance in cellular homeostasis and disease pathology. Thus, the study of RPL8 not only furthers our comprehension of fundamental cellular mechanisms but also opens new avenues for therapeutic strategies in diseases associated with ribosome dysfunction.
