Analytical Data
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Gene name
RPL30
- Application
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Alternative Names
60S ribosomal protein L30; L30; Ribosomal protein L30; RL30_HUMAN; RPL30
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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
P62888
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Expression Region
1-115aa
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Molecular Weight
39.8 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
RPL30, a member of the ribosomal protein family, plays a crucial role in the assembly and function of the ribosome, the cellular machinery responsible for protein synthesis. Research has shown that RPL30 is essential for the proper translation of mRNA into proteins, influencing cellular growth and development. Abnormalities in ribosomal proteins, including RPL30, are linked to various diseases, including cancer and ribosomal disorders such as Diamond-Blackfan anemia. The study of RPL30 recombinant proteins has gained significance as scientists aim to better understand its functional mechanisms and interactions within the ribosome. By producing RPL30 in a recombinant form, researchers can perform detailed structural and functional analyses, contributing to our knowledge of ribosome biogenesis and regulation. This research not only enhances our understanding of fundamental biological processes but also has potential implications for therapeutic strategies targeting diseases associated with ribosomal dysfunctions. Furthermore, advancements in techniques such as cryo-electron microscopy and X-ray crystallography have enabled researchers to study the structural properties of RPL30 in unprecedented detail. Understanding the role of RPL30 in the context of ribosomal assembly and function could pave the way for novel approaches in the treatment of related diseases, making it a promising area of investigation in molecular biology and medicine.
