Analytical Data
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基因名
fbaA
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简介
The fbaA protein plays a critical role in cellular metabolism by catalyzing the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerol phosphate) with glyceraldehyde 3-phosphate (G3P), leading to the formation of fructose 1,6-bisphosphate (FBP) role. This enzyme activity is essential for gluconeogenesis and glycolysis, reflecting its involvement in the conversion of key intermediates necessary for energy production and carbon flux. fbaA Protein, Shigella flexneri is the recombinant fbaA protein, expressed by E. coli , with tag free.
- Application
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别名
fbaA; Fructose-bisphosphate aldolase class 2; FBP aldolase; FBPA; Fructose-1; 6-bisphosphate aldolase; Fructose-bisphosphate aldolase class II
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种属
Others
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表达系统
E. coli
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标签
Tag Free
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P0AB73
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表达区间
M1-L359
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蛋白长度
Full Length
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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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
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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.
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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.
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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
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Protein Description
FbaA, or fructose bisphosphate aldolase A, is an important enzyme involved in the glycolytic pathway, facilitating the cleavage of fructose 1,6-bisphosphate into glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. It plays a critical role in cellular metabolism, particularly in organisms that utilize glucose as a primary energy source. Research into recombinant FbaA has gained traction due to its potential applications in biotechnology and metabolic engineering. The ability to produce FbaA in a recombinant system allows for detailed studies of its enzymatic properties, structure-function relationships, and regulatory mechanisms. Additionally, understanding the molecular basis of FbaA's activity can lead to advancements in metabolic engineering strategies aimed at optimizing microbial production processes, enhancing fermentative pathways, and developing bio-based alternatives to fossil fuels. Furthermore, recombinant FbaA can be utilized in creating biosensors for glucose detection and metabolic profiling in various organisms. Ongoing studies focus on improving the efficiency of recombinant protein expression, purification methods, and the investigation of FbaA's potential roles in different biological contexts beyond traditional glycolysis, such as in specific stress responses or metabolic adaptations. Overall, the exploration of FbaA in recombinant systems is poised to enhance our understanding of metabolic pathways and contribute to the development of innovative biotechnological applications.
