Analytical Data
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Gene name
hupA
- Application
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Alternative Names
hupA；DNA-binding Protein HU-alpha
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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
P0ACF1
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Expression Region
1-90aa
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AA Sequence
MNKTQLIDVIAEKAELSKTQAKAALESTLAAITESLKEGDAVQLVGFGTFKVNHRAERTGRNPQTGKEIKIAAANVPAFVSGKALKDAVK
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Molecular Weight
11.0 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
HupA is a protein that plays a critical role in the physiological processes of various microorganisms, particularly in the context of environmental adaptability and stress response. It serves as a subunit of the DNA-dependent RNA polymerase in certain bacteria, influencing gene expression and regulation. The study of HupA recombinant proteins has gained prominence due to their potential applications in biotechnology and medicine. By understanding the molecular structure and function of HupA, researchers aim to explore its role in microbial metabolism, biofilm formation, and pathogenesis. The recombinant expression of HupA allows scientists to produce large quantities of this protein, facilitating detailed biochemical assays and structural analyses. These studies not only shed light on the fundamental biological mechanisms governing microbial life but also open avenues for developing novel antimicrobial strategies and biotechnological applications. Furthermore, the ability to manipulate HupA through genetic engineering offers exciting prospects for enhancing microbial strains with desirable traits, contributing to advancements in bioengineering and synthetic biology. Overall, the research on HupA recombinant proteins is a significant area of investigation that bridges microbiology, molecular biology, and applied sciences, highlighting the importance of understanding microbial adaptations in various ecological and industrial contexts.
