Analytical Data
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Gene name
ihfB
- Application
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Alternative Names
ihfB；himD；hip；Integration host factor subunit beta
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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
P0A6Y1
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Expression Region
1-94aa
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AA Sequence
MTKSELIERLATQQSHIPAKTVEDAVKEMLEHMASTLAQGERIEIRGFGSFSLHYRAPRTGRNPKTGDKVELEGKYVPHFKPGKELRDRANIYG
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Molecular Weight
10.6 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
IhfB, a subunit of the integration host factor (IHF), plays a crucial role in the regulation of gene expression and DNA bending in prokaryotic organisms. As a histone-like protein, IhfB interacts with DNA to facilitate the formation of higher-order structures, influencing processes such as transcription, replication, and recombination. The study of IhfB has gained significant attention due to its essential functions in bacterial physiology and pathogenesis, making it a potential target for novel antimicrobial strategies. Researchers have been investigating the structural characteristics and functional mechanisms of IhfB to understand its interactions with DNA and other cellular components. Additionally, the recombinant expression of IhfB provides an opportunity to explore its properties in a controlled environment, enabling detailed studies on its role in DNA architecture alteration and gene regulatory networks. This research not only enhances our understanding of fundamental biological processes in bacteria but also opens avenues for biotechnological applications, such as synthetic biology and the development of therapeutic agents against pathogenic bacteria. Overall, the study of IhfB recombinant proteins is pivotal for unraveling the complexities of DNA-protein interactions and their implications in microbial ecology and evolution.
