Analytical Data
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Gene name
fabF
- Application
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Alternative Names
fabF；3-oxoacyl-[acyl-carrier-Protein] synthase. 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
P0AAI5
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Expression Region
2-413aa
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AA Sequence
SKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNGSLIFKKI
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Molecular Weight
58.9 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
FabF is a key enzyme involved in fatty acid biosynthesis, playing a critical role in the synthesis of long-chain fatty acids through the synthesis of malonyl-CoA. Understanding the structure and function of FabF is essential for elucidating metabolic pathways in various organisms, including bacteria, fungi, and plants. The recombination and expression of the FabF protein are pivotal in advancing our knowledge of fatty acid metabolism and its regulation. This knowledge has implications for biotechnological applications, such as the production of biofuels, bioplastics, and other valuable fatty acid-derived compounds. Additionally, research on FabF can contribute to the development of novel antimicrobial agents, as targeting fatty acid biosynthesis in pathogens provides a potential strategy for drug discovery. The ability to produce recombinant FabF protein allows for detailed biochemical and structural studies, facilitating insights into substrate specificity, enzymatic mechanisms, and the potential for engineering metabolic pathways for enhanced fatty acid production. Given the increasing interest in sustainable bioproducts and the importance of fatty acids in health and industry, FabF continues to be a significant target for research in metabolic engineering and synthetic biology.
