Analytical Data
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Gene name
RPL14
- Application
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Alternative Names
CAG-ISL 7
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P50914
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Expression Region
2-214aa
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Molecular Weight
50.2 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
RPL14, a ribosomal protein part of the ribosomal 60S subunit, has garnered attention in recent research due to its critical role in ribosome biogenesis and protein synthesis. As an essential component of the cellular machinery, RPL14 is implicated in various cellular processes, including growth, differentiation, and response to stress. Studies have indicated that alterations in RPL14 expression can influence cancer development and progression, making it a subject of interest in oncological research. Additionally, the increasing understanding of its involvement in the regulation of gene expression and potential role in various diseases highlights the necessity for in-depth studies on its structure and function. The recombinant expression of RPL14 facilitates the exploration of its biochemical properties, interaction networks, and impact on ribosomal dynamics. By producing RPL14 in a controlled environment, researchers can investigate its behavior in isolation and in complex cellular systems, thereby elucidating its biological significance. The availability of RPL14 as a recombinant protein also opens up opportunities for developing novel therapeutic strategies that target ribosomal function in diseases such as cancer. Overall, the ongoing investigation into RPL14 provides valuable insights into its pivotal functions within the ribosome and broader implications in health and disease.
