Analytical Data
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Gene name
fabD
- Application
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Alternative Names
fabD；MT；Malonyl-CoA-acyl carrier Protein transacylase. mitochondrial
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Species
E.coli
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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
Q5HGK3
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Expression Region
1-308aa
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AA Sequence
MSKTAIIFPGQGAQKVGMAQDLFNNNDQATEILTSAANTLDFDILETMFTDEEGKLGETENTQPALLTHSSALLAALKNLNPDFTMGHSLGEYSSLVAADVLSFEDAVKIVRKRGQLMAQAFPTGVGSMAAVLGLDFDKVDEICKSLSSDDKIIEPANINCPGQIVVSGHKALIDELVEKGKSLGAKRVMPLAVSGPFHSSLMKVIEEDFSSYINQFEWRDAKFPVVQNVNAQGETDKEVIKSNMVKQLYSPVQFINSTEWLIDQGVDHFIEIGPGKVLSGLIKKINRDVKLTSIQTLEDVKGWNEND
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Molecular Weight
35.6 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
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Protein Description
FabD is a key enzyme involved in fatty acid biosynthesis, specifically in the acyl-ACP (acyl carrier protein) synthetase family, which plays a crucial role in the metabolic pathways of various organisms, including bacteria and higher plants. As a member of this enzyme family, FabD catalyzes the conversion of malonyl-CoA to malonyl-ACP, a critical step in the synthesis of fatty acids. The study of FabD is particularly important due to its implications in microbial growth and survival, making it a target for the development of antibiotics and other antimicrobial agents. Furthermore, understanding FabD's structure and function can offer insights into the regulation of fatty acid metabolism and its impact on cellular processes, such as membrane fluidity, energy storage, and signaling pathways. The recombinant expression of FabD allows researchers to characterize its enzymatic properties, elucidate its mechanism of action, and explore its potential applications in biotechnology, including biofuel production and metabolic engineering. Overall, the investigation of FabD and its recombinant protein can provide valuable information for both fundamental biology and applied sciences, supporting efforts to manipulate fatty acid biosynthesis for various industrial and pharmaceutical purposes.
