Analytical Data
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Gene name
rpmE
- Application
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Alternative Names
rpmE；Large ribosomal subunit Protein bL31
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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
P0A7M9
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Expression Region
1-70aa
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AA Sequence
MKKDIHPKYEEITASCSCGNVMKIRSTVGHDLNLDVCSKCHPFFTGKQRDVATGGRVDRFNKRFNIPGSK
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Molecular Weight
34.9 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
RpmE is a crucial protein found in bacteria that plays a significant role in the assembly of the ribosomal 50S subunit, a fundamental component of the ribosome responsible for protein synthesis. Research on RpmE has gained traction due to its potential implications in understanding bacterial ribosome function and the development of novel antibiotics. Given the rising threat of antibiotic resistance, targeting ribosomal proteins such as RpmE presents a promising strategy for designing new therapeutic agents. The protein is known to interact with other ribosomal proteins and rRNA, contributing to the intricate process of ribosome maturation. Studies have demonstrated that mutations in the rpmE gene can lead to defects in ribosome assembly, which in turn affects bacterial growth and viability, highlighting its essential role in cellular biology. Moreover, the conservation of RpmE across various bacterial species suggests that it may serve as a universal target for antibiotic development. Investigating the structure and function of RpmE can provide insights into the fundamental mechanisms of ribosome assembly and offer opportunities for innovative approaches in combating bacterial infections. Overall, the study of RpmE and its dynamics within the ribosomal environment is poised to contribute significantly to both microbiology and antibiotic research.
