Analytical Data
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Gene name
hfq
- Application
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Alternative Names
(HF-1)(Host factor-I protein)(HF-I)
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0A6X3
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Expression Region
2-102aa
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Molecular Weight
18.5 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
Hfq, an RNA-binding protein found in various bacteria, plays a crucial role in post-transcriptional gene regulation by facilitating the interaction between small non-coding RNAs (sRNAs) and their target mRNAs. The research into Hfq and its recombinant protein has gained significant attention due to its involvement in essential cellular processes such as stress response, virulence, and biofilm formation. Hfq operates as a molecular chaperone that stabilizes sRNAs, enhancing their ability to modulate gene expression by base-pairing with complementary mRNA sequences. This functionality is pivotal in adapting to environmental changes, making Hfq a vital component in bacterial survival strategies. Furthermore, its importance is highlighted in the context of antibiotic resistance, as understanding Hfq's mechanisms can provide insights for novel therapeutic approaches. Researchers are increasingly interested in recombinant Hfq proteins to dissect its structure-function relationships, explore its interactions with sRNAs and mRNAs, and develop biotechnological applications. The production of Hfq in a recombinant form allows for detailed biochemical analysis and potential utilization in synthetic biology. Overall, the study of Hfq and its recombinant forms is essential for advancing our knowledge of bacterial regulatory mechanisms and could contribute to innovative strategies for controlling pathogenic bacteria.
