Analytical Data
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Gene name
rplV
- Application
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Alternative Names
rplV；eryB；Large ribosomal subunit Protein uL22
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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
Q2GL54
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Expression Region
1-112aa
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AA Sequence
MSIVIAAKGLGLRSTPAKLNLVADLIRGKDVAVAAMYLKFCKKKAALLIDKVLKSAIANARANYGVDADNLYVKEVLVGKAFTLRRVQPRARGRACRISKRYGSVVVKLLER
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Molecular Weight
17.2 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
RplV, a component of the 50S ribosomal subunit, plays a crucial role in bacterial protein synthesis, making it a significant target in antibiotic research. The study of RplV recombinant protein is driven by its potential to aid in understanding the mechanisms of ribosomal function and the development of novel antimicrobial agents. In recent years, increasing antibiotic resistance among pathogenic bacteria has highlighted the urgent need for new therapeutic strategies. By exploring the structure and function of RplV, researchers aim to identify specific interactions within the ribosome that can be disrupted by new drugs, thereby inhibiting bacterial growth. Furthermore, the production of RplV recombinant proteins in suitable expression systems allows for detailed biochemical and structural analyses, paving the way for high-throughput screening of compounds that can selectively target bacterial ribosomes. This research not only enhances our fundamental understanding of ribosome biology but also holds promise for addressing the critical challenge of antibiotic resistance, offering hope for the development of effective treatments against resistant strains of bacteria.
