Analytical Data
-
基因名
acnB
-
简介
The acnB protein coordinates short-chain fatty acid catabolism through the TCA pathway and 2-methylcitric acid cycle I, demonstrating catalytic versatility. It is involved in the reversible isomerization of citric acid to isocitrate and the hydration of 2-methyl-cis-aconitic acid. acnB Protein, E. coli is the recombinant Virus-derived acnB protein, expressed by E. coli , with tag free.
- Application
-
别名
Aconitate hydratase B; ACN; Aconitase; RNA-binding protein; acnB; yacI; yacJ
-
种属
Virus
-
表达系统
E. coli
-
标签
Tag Free
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P36683
-
表达区间
M1-V865
-
蛋白长度
Full Length
-
分子量
95 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 study of acnB recombinant protein is grounded in its critical role in bacterial metabolism, particularly in the context of energy production and metabolic pathways. AcnB, or aconitase, is an important enzyme that catalyzes the isomerization of citrate to isocitrate in the tricarboxylic acid (TCA) cycle, which is essential for aerobic respiration in many microorganisms. Research into acnB not only enhances our understanding of fundamental metabolic processes but also sheds light on the regulatory mechanisms that bacteria employ to adapt to varying environmental conditions. Moreover, dysfunctions or alterations in acnB expression have been linked to various pathogenic traits in bacteria, making it a potential target for therapeutic interventions. By investigating acnB recombinant proteins through techniques like gene cloning and expression in heterologous systems, researchers aim to characterize its enzymatic properties, structural features, and regulatory roles in metabolic pathways. These studies have significant implications for biotechnology, microbial ecology, and the development of antimicrobial agents, as they could lead to novel strategies for controlling bacterial growth in both industrial and clinical settings. The detailed understanding of acnB's function further contributes to the broader knowledge of metabolic engineering, aiding in the design of more efficient microbial strains for various applications in bioproduction and bioremediation.












