Analytical Data
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Gene name
rplI
- Application
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Alternative Names
rplI；Large ribosomal subunit Protein bL9
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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
P0A7R1
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Expression Region
1-144aa
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AA Sequence
MQVILLDKVANLGSLGDQVNVKAGYARNFLVPQGKAVPATKKNIEFFEARRAELEAKLAEVLAAANARAEKINALETVTIASKAGDEGKLFGSIGTRDIADAVTAAGVEVAKSEVRLPNGVLRTTGEHEVSFQVHSEVFAKVIV
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Molecular Weight
42.3 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
The study of the rplI recombinant protein is situated within the broader context of ribosomal protein research, which is vital for understanding fundamental cellular processes such as protein synthesis and gene regulation. RplI, a component of the large ribosomal subunit, plays a crucial role in the assembly and function of ribosomes, the cellular machinery responsible for translating mRNA into proteins. Given the importance of ribosomes in cellular biology, alterations in ribosomal proteins like RplI can have significant implications for cell growth, development, and response to environmental stressors. Furthermore, research has demonstrated that mutations or dysregulation of ribosomal proteins can contribute to various diseases, including cancer and genetic disorders. The recombinant expression of RplI not only facilitates detailed biochemical analyses but also offers potential insights into its structure and function. By studying this protein in the context of ribosome assembly and function, researchers aim to unravel the complexities of translational control and its impact on cellular physiology. Overall, the exploration of rplI and its associated pathways holds promise for advancing our understanding of ribosome biology and developing therapeutic strategies for diseases linked to ribosomal dysfunction.
