Analytical Data
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Gene name
RPS25
- Application
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Alternative Names
RPS25；Small ribosomal subunit Protein eS25
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Species
Human
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Source
E. coli
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Tag
His Tag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P62851
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Expression Region
1-125aa
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AA Sequence
MPPKDDKKKKDAGKSAKKDKDPVNKSGGKAKKKKWSKGKVRDKLNNLVLFDKATYDKLCKEVPNYKLITPAVVSERLKIRGSLARAALQELLSKGLIKLVSKHRAQVIYTRNTKGGDAPAAGEDA
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Molecular Weight
14.5kDa
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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
Identification
Protein Description
RPS25, a crucial component of the ribosomal small subunit, plays a significant role in protein synthesis within eukaryotic cells. As a ribosomal protein, RPS25 is essential for the assembly and stability of ribosomes, which are the cellular machines responsible for translating messenger RNA into proteins. Research into RPS25 has gained momentum due to its implications in various cellular processes and its potential links to diseases, including cancer. Alterations in ribosomal proteins, such as RPS25, can lead to dysregulated protein synthesis, contributing to oncogenesis and other pathologies. Moreover, the study of RPS25 has been enhanced by advances in recombinant DNA technology, allowing for the production of RPS25 as a recombinant protein. This presents opportunities for detailed structural and functional analyses, facilitating a better understanding of its mechanisms in ribosome biogenesis and function. Investigating the characteristics and interactions of RPS25 can reveal insights into the complexities of ribosome assembly and its impact on cellular health. Additionally, understanding the role of RPS25 in the context of translational control and its potential as a therapeutic target remains a compelling area of research in molecular biology and medicine. Thus, the exploration of RPS25 not only enriches our knowledge of fundamental biological processes but also paves the way for potential applications in disease treatment and biotechnology.
