Analytical Data
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Gene name
RPL17
- Application
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Alternative Names
60S ribosomal protein L23;PD-1
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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
P18621
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Expression Region
2-184aa
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Molecular Weight
48.3 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
RPL17, a member of the ribosomal protein family, plays a critical role in ribosome biogenesis and protein synthesis. As a component of the 60S ribosomal subunit, RPL17 is essential for the assembly of ribosomal RNA and proteins, contributing to the translation process in cells. Recent studies have highlighted its involvement not only in fundamental cellular functions but also in various pathological conditions, including cancer and genetic disorders. Given its pivotal role in ribosome function and cellular homeostasis, the overexpression or dysregulation of RPL17 has been linked to tumorigenesis and cancer progression. Consequently, researchers are increasingly focusing on the recombinant expression and characterization of RPL17 to elucidate its structure-function relationship and potential as a therapeutic target. By generating RPL17 recombinant proteins through advanced molecular biology techniques, scientists aim to investigate its interactions with other ribosomal components and regulatory proteins, providing insights into the ribosomal assembly process and its implications in diseases. Understanding RPL17's role at the molecular level could pave the way for novel strategies in cancer treatment and may also enhance our knowledge of ribosome-related disorders.
