Analytical Data
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Gene name
DNA-binding 蛋白 HU-alpha
- Application
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Alternative Names
HU-2 NS2
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Species
Escherichia coli O157:H7
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0ACF2
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Expression Region
1-90aa
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Molecular Weight
25.5 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
HU-alpha, a DNA-binding protein, plays a crucial role in bacterial DNA organization and protection. It is a major component of the nucleoid in prokaryotes, where it facilitates the compaction of DNA and regulates gene expression by interacting with various DNA structures. The study of recombinant HU-alpha protein is significant for elucidating its function and mechanism in DNA-protein interactions. Understanding HU-alpha's binding affinity, specificity, and structural dynamics can provide insights into its role in DNA replication, repair, and transcription. Furthermore, investigating HU-alpha interactions can shed light on bacterial pathogenesis and the development of novel antimicrobial strategies. As a model system, recombinant HU-alpha allows researchers to perform a range of biophysical and biochemical analyses, enhancing our knowledge of nucleoid organization and the fundamental principles governing protein-DNA interactions in cells. Research on HU-alpha also offers potential applications in biotechnology, including the design of DNA-based materials and tools for genetic engineering. Overall, the exploration of HU-alpha provides a valuable perspective on the molecular mechanisms underpinning DNA management in bacteria, contributing to our broader understanding of cellular processes and the evolution of genomic architectures.
