Analytical Data
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Gene name
fabG
- Application
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Alternative Names
fabG；3-oxoacyl-[acyl-carrier-Protein] reductase FabG
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGMYMV
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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, also known as β-ketoacyl-ACP reductase, is an essential enzyme in the fatty acid biosynthesis pathway, catalyzing the reduction of β-ketoacyl acyl carrier protein (ACP) to yield acyl-ACP. This reaction is a critical step in the metabolic pathway that synthesizes fatty acids, which are vital components of cellular membranes and energy storage molecules. Understanding the structure and function of FabG is pivotal, as it offers insights into the regulatory mechanisms of fatty acid metabolism and can inform the development of antibiotics, given that fatty acid biosynthesis is a prime target in bacterial pathogens. The research on recombinant FabG proteins involves the molecular cloning and expression of the fabG gene in various host systems, often leading to the production of the enzyme in substantial quantities for further characterization. These studies aim to elucidate the enzyme's kinetic properties, substrate specificity, and structural features using techniques such as X-ray crystallography and NMR spectroscopy. Moreover, recombinant FabG can be used in metabolic engineering applications to enhance fatty acid production in microbial hosts, thus contributing to biofuel and biodegradable polymer industries. The recent advancements in synthetic biology and protein engineering have further opened avenues for modulating FabG activity and stability, thereby enhancing our understanding of its role in metabolic pathways and its potential industrial applications.
