Analytical Data
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Gene name
hup
- Application
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Alternative Names
hup；HUP2；Paired box Protein Pax-3
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Species
Human
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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
P0C0H2
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Expression Region
1-91aa
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AA Sequence
MANKQDLIAKVAEATELTKKDSAAAVDAVFSTIEAFLAEGEKVQLIGFGNFEVRERAARKGRNPQTGAEIEIAASKVPAFKAGKALKDAVK
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Molecular Weight
17.1 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
Related Products
Protein Description
The study of Hup (hydrogenase upstream) recombinant proteins has gained significant attention due to their critical roles in various biological processes, particularly in photosynthetic organisms and certain bacteria. Hup proteins are associated with hydrogen production and are often involved in metabolic pathways that enhance energy efficiency and sustainability. The drive towards renewable energy sources has emphasized the importance of understanding these proteins, as they can facilitate the development of biohydrogen production systems. Recombinant DNA technology enables the expression and characterization of Hup proteins in various model organisms, allowing researchers to elucidate their structure, function, and mechanisms of action. This research not only contributes to basic biochemical knowledge but also has practical applications in bioengineering and the design of microbial systems for sustainable energy generation. Moreover, the exploration of Hup protein interactions and regulatory pathways can offer insights into how organisms adapt to fluctuating environmental conditions, providing a broader understanding of metabolic flexibility in microbial communities. As such, research on Hup recombinant proteins stands at the intersection of microbiology, biochemistry, and renewable energy technology, highlighting their potential for advancing both fundamental science and practical applications in addressing global energy challenges.
