Analytical Data
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Gene name
hypA
- Application
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Species
Clostridium perfringens
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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
Q46205
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Expression Region
206-390aa
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Molecular Weight
28.6 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
Related Products
Protein Description
The hypA gene is known to be involved in the synthesis of hydrogen gas in certain bacteria, particularly in the context of nickel-dependent enzymes. Research into the hypA gene and its corresponding protein, hypA, has gained traction due to its potential applications in bioenergy and bioremediation. Many microorganisms have developed unique strategies to utilize nickel as a cofactor for hydrogenase enzymes, which play a crucial role in the hydrogen production process. Understanding the functionality and the structural biology of the hypA protein can provide insights into its role in nickel transport and utilization, as well as hydrogen metabolism. Additionally, the recombinant expression of hypA protein allows for detailed studies on its biochemical properties and interactions, paving the way for engineering microbes that can efficiently convert substrates into hydrogen gas. This has significant implications for renewable energy production and addressing environmental challenges, making hypA a focal point in microbiological and biochemical research. As scientists continue to unravel the complex pathways involving hypA, its study may lead to innovative strategies for harnessing biological systems for sustainable energy solutions.
