Analytical Data
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Gene name
rplB
- Application
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Alternative Names
rplB；Large ribosomal subunit Protein uL2
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Species
Human
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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
P60422
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Expression Region
2-273aa
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AA Sequence
AVVKCKPTSPGRRHVVKVVNPELHKGKPFAPLLEKNSKSGGRNNNGRITTRHIGGGHKQAYRIVDFKRNKDGIPAVVERLEYDPNRSANIALVLYKDGERRYILAPKGLKAGDQIQSGVDAAIKPGNTLPMRNIPVGSTVHNVEMKPGKGGQLARSAGTYVQIVARDGAYVTLRLRSGEMRKVEADCRATLGEVGNAEHMLRVLGKAGAARWRGVRPTVRGTAMNPVDHPHGGGEGRNFGKHPVTPWGVQTKGKKTRSNKRTDKFIVRRRSK
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Molecular Weight
36.7 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
RplB, a crucial component of the ribosomal RNA core structure, is an essential ribosomal protein in bacteria that plays a significant role in the assembly and function of the ribosome. It is encoded by the rplB gene and is involved in protein synthesis, serving not only as a structural element but also as a participant in the ribosomal activity. Studies on RplB have gained attention due to its potential implications in antibiotic resistance; many antibiotics target ribosomal functions, and mutations or alterations in RplB can lead to resistance mechanisms in pathogenic bacteria. Understanding the structural and functional characteristics of RplB is vital for elucidating the mechanisms of ribosome assembly and the interplay between ribosomal proteins and ribosomal RNA. Furthermore, the recombinant expression of RplB allows researchers to investigate its properties in vitro, facilitating studies on its interactions with ribosomal RNA and other ribosomal proteins. This research has significant implications for developing new antibiotic strategies and understanding bacterial ribosome biogenesis. Additionally, RplB serves as a model for studying the evolutionary dynamics of ribosomal components across different species, contributing to our knowledge of molecular evolution and the foundational aspects of biological systems. Thus, the study of RplB not only enhances our understanding of fundamental cellular processes but also provides insights into potential therapeutic targets for combating antibiotic-resistant bacterial infections.
