Analytical Data
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Gene name
fabI
- Application
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Alternative Names
fabI；FABPI；Fatty acid-binding Protein. intestinal
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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
P0AEK5
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Expression Region
2-262aa
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AA Sequence
GFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIAAMNELELK
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Molecular Weight
31.8 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
FabI, an essential enzyme involved in the fatty acid biosynthesis pathway, has garnered significant attention in the field of microbiology and drug discovery due to its crucial role in bacterial cell membrane formation. As a member of the enoyl-acyl carrier protein reductase family, FabI catalyzes the reduction of enoyl-ACP to the corresponding acyl-ACP, making it a vital player in the synthesis of long-chain fatty acids. This function is particularly important in pathogenic bacteria, where fatty acid composition directly influences virulence and survival. Recent studies have identified FabI as a promising target for antibiotic development, especially considering the rising rates of antibiotic resistance among common bacterial pathogens. Researchers have employed various recombinant DNA techniques to express and purify FabI protein, facilitating the study of its enzymatic activity, structure, and potential inhibitors. By understanding the mechanisms that regulate FabI activity and its interaction with different substrates and inhibitors, scientists aim to develop novel antimicrobial agents that can circumvent existing resistance mechanisms. The exploration of FabI's role not only enhances our knowledge of bacterial metabolism but also serves as a foundation for innovative therapeutic strategies against resistant bacterial strains.
