Analytical Data
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Gene name
RPL30
- Application
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Alternative Names
RPL30;Large ribosomal subunit Protein eL30
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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
P62888
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Expression Region
1-115aa
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AA Sequence
MVAAKKTKKSLESINSRLQLVMKSGKYVLGYKQTLKMIRQGKAKLVILANNCPALRKSEIEYYAMLAKTGVHHYSGNNIELGTACGKYYRVCTLAIIDPGDSDIIRSMPEQTGEK
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Molecular Weight
39.8kDa
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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
RPL30, or Ribosomal Protein L30, is an essential component of the large ribosomal subunit, playing a vital role in protein synthesis within the cell. Its function extends beyond ribosome assembly, influencing various cellular processes, including cell proliferation and stress response. Recent studies have highlighted the significance of RPL30 in various diseases, particularly cancers, as its expression levels can be altered in malignant cells, leading to dysregulated protein synthesis. Researchers have turned their attention to the recombinant production of RPL30 to facilitate extensive studies on its structure and function. By generating RPL30 in a controlled laboratory setting, scientists can investigate its interactions with RNA and other ribosomal proteins, elucidating the mechanisms of ribosome assembly and function. Additionally, recombinant RPL30 is advantageous for potential therapeutic applications, as understanding its role in ribosomal biogenesis may reveal novel targets for anti-cancer therapies. Overall, the exploration of RPL30 as a recombinant protein serves as a crucial step in advancing our understanding of ribosomal dynamics and its implications in health and disease.
