Analytical Data
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Gene name
fabG
- Application
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Alternative Names
(3-ketoacyl-acyl carrier protein reductase)(Beta-Ketoacyl-acyl carrier protein reductase)(Beta-ketoacyl-ACP reductase)
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Species
Escherichia coli
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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
P0AEK2
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Expression Region
1-244aa
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Molecular Weight
33.0 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
FabG, a key enzyme in the fatty acid biosynthesis pathway, plays a crucial role in converting 3-ketoacyl-ACP to hydroxyacyl-ACP, a vital step for the synthesis of fatty acids. This enzyme has garnered significant attention in both microbiology and biotechnology due to its potential applications in biocatalysis and the production of biofuels and bio-based products. Research on fabG has expanded in recent years, driven by the increasing demand for sustainable alternatives to fossil fuels and the need for efficient microbial production systems. Various studies have focused on the characterization, expression, and functional analysis of recombinant FabG proteins from different organisms, including bacteria and plants, to enhance understanding of their catalytic mechanisms and optimize their activity for industrial applications. The exploration of fabG's role in different metabolic contexts has also provided insights into its regulatory mechanisms and interactions within the metabolic network. By engineering fabG through techniques such as site-directed mutagenesis and protein engineering, researchers aim to improve its substrate specificity and reaction efficiency, thereby facilitating the utilization of renewable resources for fatty acid production. Additionally, understanding the evolutionary aspects of fabG across diverse species can inform strategies for enzyme optimization and the development of innovative bioprocesses. Overall, the study of fabG recombinant proteins is poised to contribute significantly to sustainable biomanufacturing and metabolic engineering advancements.
