Analytical Data
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Gene name
RPL9
- Application
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Alternative Names
RPL9；RPL9P7；RPL9P8；RPL9P9；Large ribosomal subunit Protein uL6
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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
P32969
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Expression Region
1-192aa
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AA Sequence
MKTILSNQTVDIPENVDITLKGRTVIVKGPRGTLRRDFNHINVELSLLGKKKKRLRVDKWWGNRKELATVRTICSHVQNMIKGVTLGFRYKMRSVYAHFPINVVIQENGSLVEIRNFLGEKYIRRVRMRPGVACSVSQAQKDELILEGNDIELVSNSAALIQQATTVKNKDIRKFLDGIYVSEKGTVQQADE
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Molecular Weight
48.9 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
RPL9, also known as ribosomal protein L9, is a crucial component of the ribosomal machinery involved in protein synthesis in eukaryotic cells. As a member of the large ribosomal subunit, RPL9 plays a significant role in ribosome assembly and function, impacting translational accuracy and efficiency. Recent studies have suggested that RPL9 is not only vital for conventional protein synthesis but also participates in various cellular processes, including cell proliferation, stress responses, and apoptosis. Its expression levels have been linked to several diseases, including cancer, where alterations in ribosomal proteins can affect the overall translational landscape, leading to dysregulated protein expression. Therefore, the recombinant expression of RPL9 serves as a valuable tool for deciphering its functional roles in both normal and pathophysiological contexts. By producing RPL9 as a recombinant protein, researchers can investigate its structure, interactions with other ribosomal components, and its regulatory pathways. This opens avenues for developing targeted therapies that could mitigate the effects of RPL9 dysregulation in disease models, thereby enhancing our understanding of ribosome biology and its implications in health and disease. The ongoing research into RPL9 and its recombinant protein forms is thus essential for advancing our knowledge of cellular mechanisms and potential therapeutic strategies.
