Analytical Data
-
基因名
NDUFA12
- Application
-
别名
13KDA differentiation-associated protein Complex I-B17.2
-
种属
Human
-
表达系统
E. coli
-
标签
N- GST
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q9UI09
-
表达区间
1-145aa
-
分子量
44.1 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
NDUFA12, a gene encoding a subunit of the mitochondrial respiratory chain complex I (NADH:ubiquinone oxidoreductase), plays a crucial role in oxidative phosphorylation, a fundamental process for ATP production in eukaryotic cells. The study of NDUFA12 recombinant protein is significant due to its implications in mitochondrial function and energy metabolism. Deficiencies or mutations in NDUFA12 have been linked to various mitochondrial diseases, leading to metabolic dysfunction and neurodegenerative disorders. By expressing and characterizing recombinant NDUFA12, researchers aim to gain deeper insights into its structural and functional properties, elucidating its role in complex I assembly and stability. Furthermore, understanding the biochemical pathways involving NDUFA12 can contribute to developing therapeutic strategies for mitochondrial diseases. Recent advances in recombinant protein technology and structural biology allow for detailed studies, enabling the exploration of NDUFA12 interactions with other subunits and cofactors involved in mitochondrial respiration. Such research not only furthers our understanding of mitochondrial bioenergetics but also highlights the potential for targeted interventions in mitochondrial dysfunction-related diseases.
