Analytical Data
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Gene name
csrA
- Application
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Alternative Names
csrA；sow；yviG；Translational regulator CsrA
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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
B1XCM4
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Expression Region
1-61aa
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AA Sequence
MLILTRRVGETLMIGDEVTVTVLGVKGNQVRIGVNAPKEVSVHREEIYQRIQAEKSQQSSY
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Molecular Weight
6.9 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
csrA is a key regulatory protein in bacteria, particularly in Escherichia coli, known for its role in post-transcriptional regulation of gene expression. It is involved in various physiological processes, including biofilm formation, virulence, and stress responses. Research has shown that csrA binds to specific RNA motifs, influencing the stability and translation of target mRNAs, thus playing a critical role in bacterial adaptation to environmental changes. Understanding the molecular mechanisms of csrA can provide insights into bacterial behavior and pathogenicity, making it a significant target for antibiotic development. Recent studies have focused on the recombinant expression of csrA to analyze its structure and function in detail. By producing this protein in a controlled environment, researchers aim to characterize its interactions with RNA and other molecular partners, elucidating its regulatory networks. Furthermore, investigating csrA in different bacterial strains can reveal its conservation and variation, contributing to a broader understanding of bacterial regulatory systems. Such research not only enhances our knowledge of bacterial physiology but also opens avenues for potential therapeutic interventions against bacterial infections.
