Analytical Data
-
基因名
hypA
- Application
-
种属
Clostridium perfringens
-
表达系统
E. coli
-
标签
N- His & C- Myc
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q46205
-
表达区间
206-390aa
-
分子量
28.6 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
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.
-
保存条件 & 期限
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.
-
运输条件
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.
