Analytical Data
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Gene name
fabH
- Application
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Alternative Names
3-oxoacyl-[acyl-carrier-protein] synthase III;Beta-ketoacyl-ACP synthase III; KAS III
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Species
Staphylococcus aureus
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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
Q5HHA2
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Expression Region
1-313aa
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Molecular Weight
41.3 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
FabH (fatty acid biosynthesis enzyme) is a key enzyme in the fatty acid synthesis pathway, playing a pivotal role in the initial step of fatty acid biosynthesis in various organisms, including bacteria and plants. The enzyme catalyzes the condensation of acyl-CoA and malonyl-CoA to form β-ketoacyl-ACP, which is crucial for the elongation of fatty acids. Understanding FabH is crucial due to its potential applications in biotechnology and synthetic biology, where engineered fatty acid pathways can lead to the production of biofuels, bioplastics, and other valuable chemicals. Furthermore, the exploration of FabH through recombinant protein techniques allows researchers to investigate its structure-function relationships and mechanisms of action, potentially leading to the development of new antibiotics targeting fatty acid synthesis in pathogens. The production of recombinant FabH in suitable expression systems enhances the availability of this enzyme for biophysical characterization and kinetic studies, facilitating the design of inhibitors or novel enzymes with altered specificities. Overall, studying FabH not only provides insight into essential metabolic pathways but also opens the door for innovative solutions to meet the growing demand for sustainable bio-based products.
