Analytical Data
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Gene name
rplI
- Application
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Alternative Names
rplI; b4203; JW4161; 50S ribosomal protein L9; Large ribosomal subunit protein bL9
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Species
Escherichia coli
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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
P0A7R1
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Expression Region
1-144aa
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Molecular Weight
42.3 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
The study of RplI (ribosomal protein L9) recombinant protein is rooted in the critical role that ribosomal proteins play in protein synthesis and cellular function. As essential components of ribosomes, RplI is involved in the assembly of ribosomal subunits and the translation of mRNA into proteins, which are fundamental processes in all living organisms. Current research has demonstrated that abnormalities in ribosomal proteins, including RplI, can be linked to various diseases, including cancer and ribosomopathies. Furthermore, RplI's unique structural characteristics and interactions with other ribosomal components present valuable insights into the mechanisms of translation and antibiotic targeting. Scientists employ various recombinant DNA techniques to produce RplI in cultured cells, allowing for detailed studies of its structure, function, and interactions. Understanding RplI at the molecular level not only enhances our knowledge of ribosome biogenesis and function but also aids in the development of novel therapeutic strategies targeting ribosomal dysfunctions. As a result, RplI and its recombinant variants have become subjects of extensive research within molecular biology and biochemistry, contributing to the broader understanding of cell biology and disease pathogenesis.
