Analytical Data
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Gene name
RPL26
- Application
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Alternative Names
RPL26;Large ribosomal subunit Protein uL24
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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
P61254
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Expression Region
1-145aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKFNPFV TSDRSKNRKR HFNAPSHIRR KIMSSPLSKE LRQKYNVRSM PIRKDDEVQV VRGHYKGQQI GKVVQVYRKK YVIYIERVQR EKANGTTVHV GIHPSKVVIT RLKLDKDRKK ILERKAKSRQ VGKEKGKYKE ETIEKMQE
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Molecular Weight
20 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
RPL26, a ribosomal protein that is part of the 60S subunit of the ribosome, has garnered increasing attention due to its pivotal role in protein synthesis and cellular functions. Recent studies have highlighted its involvement in various biological processes, including translation regulation, stress response, and cell proliferation. Defects in RPL26 have been implicated in several diseases, including cancer, where it can influence tumor growth and response to therapy. As a fundamental component of the ribosome, RPL26 not only contributes to the structural integrity of ribosomes but also participates in the regulation of mRNA translation, making it a crucial factor in gene expression. The investigation of RPL26, particularly through recombinant protein techniques, allows researchers to delve deeper into its functional dynamics, interactions with other ribosomal and non-ribosomal proteins, and its impact on cellular mechanisms. Furthermore, the recombinant expression of RPL26 provides a platform for studying its post-translational modifications and how these modifications affect its function in various cellular contexts. Understanding the nuances of RPL26's role could lead to novel therapeutic strategies, particularly in cancer treatment, where modulation of its activity may restore normal cellular functions. Thus, the study of RPL26 not only enhances our understanding of ribosomal biology but also opens new avenues for biomedical research, especially in the quest for targeted interventions in ribosome-related diseases.
