Analytical Data
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Gene name
RPL12
- Application
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Alternative Names
RPL12;Large ribosomal subunit Protein uL11
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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
P30050
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Expression Region
1-165aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPPKFDP NEIKVVYLRC TGGEVGATSA LAPKIGPLGL SPKKVGDDIA KATGDWKGLR ITVKLTIQNR QAQIEVVPSA SALIIKALKE PPRDRKKQKN IKHSGNITFD EIVNIARQMR HRSLARELSG TIKEILGTAQ SVGCNVDGRH PHDIIDDINS GAVECPAS
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Molecular Weight
20 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
RPL12, a ribosomal protein component of the 60S subunit, plays a crucial role in protein synthesis and cellular function. Research into RPL12 has gained attention due to its implications in various biological processes and disease mechanisms. Studies have shown that RPL12 is involved in the maintenance of ribosome integrity and is essential for proper ribosome assembly, which is vital for efficient protein translation. Abnormalities in RPL12 expression or function have been linked to several disorders, including certain types of cancer and developmental diseases. The protein's involvement in the regulation of cellular stress responses and its potential role in the modulation of gene expression have further broadened its significance in cellular biology. Recent advancements in recombinant protein technology have allowed for the production and study of RPL12 in more detail, facilitating investigations into its functional properties and interactions with other cellular components. By utilizing techniques such as gene cloning and protein purification, researchers aim to better understand the structural and functional roles of RPL12, which may ultimately reveal new therapeutic targets for diseases associated with ribosomal dysfunction. Overall, the study of RPL12 as a recombinant protein is essential for uncovering its biological significance and potential implications in health and disease.
