Analytical Data
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Gene name
rpmA
- Application
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Alternative Names
rpmA；Large ribosomal subunit Protein bL27
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Species
E.coli
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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
P0A7L8
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Expression Region
2-85aa
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AA Sequence
AHKKAGGSTRNGRDSEAKRLGVKRFGGESVLAGSIIVRQRGTKFHAGANVGCGRDHTLFAKADGKVKFEVKGPKNRKFISIEAE
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Molecular Weight
36.0 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
The study of the rpmA gene, which encodes the ribosomal protein L27 in bacteria, is significant due to its crucial role in protein synthesis and ribosome function. Ribosomal proteins play essential roles in the assembly, structural integrity, and overall functionality of ribosomes, the cellular machinery responsible for translating mRNA into proteins. Intriguingly, mutations or deletions in the rpmA gene can lead to defective ribosome assembly, impacting cellular growth and viability. Given the rising issue of antibiotic resistance, understanding the biochemical mechanisms of ribosomal proteins like RpmA can provide insights into developing novel antibiotics targeting bacterial protein synthesis. Furthermore, recombinant RpmA protein can be produced and studied to elucidate its structural characteristics and interactions within the ribosomal context. This research not only enhances our comprehension of bacterial ribosome assembly but also sets the foundation for potential therapeutic strategies against pathogenic bacteria. By exploring the functional dynamics of RpmA, researchers aim to contribute to the broader field of microbiology and antibiotic development, addressing critical challenges in infectious disease management.
