Analytical Data
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Gene name
rpmB
- Application
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Alternative Names
rpmB；Large ribosomal subunit Protein bL28
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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
P0A7M2
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Expression Region
2-78aa
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AA Sequence
SRVCQVTGKRPVTGNNRSHALNATKRRFLPNLHSHRFWVESEKRFVTLRVSAKGMRVIDKKGIDTVLAELRARGEKY
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Molecular Weight
35.9 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
Related Products
Protein Description
RpmB, a ribosomal protein of the L20 family, plays a crucial role in the assembly and function of the ribosome in bacteria. As an essential component of the 50S ribosomal subunit, RpmB is involved in stabilizing the structure of the ribosome and facilitating protein synthesis. Its importance is underscored by the fact that many antibiotics target ribosomal components, making RpmB a potential candidate for drug discovery. Research into RpmB includes studies on its structure, function, and interactions with RNA and other ribosomal proteins, which are vital for understanding the intricate processes of translation and ribosome biogenesis. Additionally, the characterization of RpmB can provide insights into evolutionary biology and the development of novel antimicrobial agents. The recombinant production of RpmB enables detailed biophysical and biochemical studies, including crystallography and NMR spectroscopy, which can reveal conformational dynamics and binding affinities. Investigating RpmB not only advances our knowledge of ribosomal biology but also opens avenues for therapeutic interventions against bacterial infections, particularly in the context of rising antibiotic resistance. Overall, the research surrounding RpmB serves as a significant contribution to molecular microbiology and biochemistry, emphasizing the need for continued exploration of ribosomal components in the fight against pathogenic bacteria.
