Analytical Data
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Gene name
RpL10
- Application
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Alternative Names
QM protein homolog (dQM) (Qm)
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Species
Drosophila melanogaster
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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
O61231
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Expression Region
1-218aa
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Molecular Weight
29.5 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
RPL10, a ribosomal protein, is a vital component of the 60S subunit of the eukaryotic ribosome, playing a crucial role in protein synthesis. Recent research has highlighted the significance of RPL10 in various biological processes, including cell proliferation, differentiation, and apoptosis. Mutations in the RPL10 gene have been linked to several malignancies, particularly pediatric acute leukemia and a subset of other cancers, suggesting its role in tumorigenesis. These mutations often lead to aberrant protein functions, which can disrupt normal ribosomal assembly and translation fidelity. Investigating the structure-function relationship of RPL10 and its mutations can offer insights into the molecular mechanisms underlying these diseases. Moreover, RPL10 has been associated with potential therapeutic targets, as its alteration may impact the effectiveness of certain treatments. Thus, understanding RPL10 and its variants not only contributes to the basic knowledge of ribosomal biology but also holds promise for developing novel strategies in cancer treatment. Current research efforts are focused on elucidating the precise mechanisms through which RPL10 mutations influence ribosome function and contribute to oncogenesis, thereby paving the way for innovative therapeutic approaches aimed at restoring normal ribosomal activity in affected individuals.
