Analytical Data
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Gene name
RPL17
- Application
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Alternative Names
RPL17；Large ribosomal subunit Protein uL22
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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
P18621
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Expression Region
2-184aa
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AA Sequence
VRYSLDPENPTKSCKSRGSNLRVHFKNTRETAQAIKGMHIRKATKYLKDVTLQKQCVPFRRYNGGVGRCAQAKQWGWTQGRWPKKSAEFLLHMLKNAESNAELKGLDVDSLVIEHIQVNKAPKMRRRTYRAHGRINPYMSSPCHIEMILTEKEQIVPKPEEEVAQKKKISQKKLKKQKLMARE
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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
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Protein Description
RPL17, a crucial ribosomal protein, is part of the 60S subunit of the eukaryotic ribosome and plays an essential role in protein synthesis. Research into RPL17 has garnered attention due to its involvement in various cellular processes and its implications in human health, particularly in cancer studies. Abnormal expression levels of RPL17 have been associated with tumorigenesis and the progression of several malignancies, indicating its potential as a biomarker for cancer diagnosis and prognosis. Moreover, RPL17 has been implicated in the regulation of the cell cycle and apoptosis, demonstrating its significance in maintaining cellular homeostasis. Given these critical functions, the study of recombinant RPL17 protein, including its structure and interactions, is essential to understand its role in ribosome assembly and function. This research may reveal novel insights into the molecular mechanisms underlying diseases and contribute to the development of therapeutic strategies, including targeted treatments in cancer and other disorders linked to ribosomal dysfunction. The recombinant production of RPL17 allows for detailed biochemical assays and structural analysis, facilitating the exploration of its functional properties and interactions with other ribosomal components. Furthermore, understanding the precise mechanisms by which RPL17 influences ribosome activity could lead to advancements in bioengineering and synthetic biology. Overall, the investigation of RPL17 as a recombinant protein holds significant promise for elucidating its biological roles and therapeutic potential, reinforcing the importance of ribosome biology in health and disease.
