Analytical Data
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Gene name
fadL
- Application
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Alternative Names
fadL；ttr；Long-chain fatty acid transport Protein
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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
Q8XCN6
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Expression Region
26-446aa
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AA Sequence
AGFQLNEFSSSGLGRAYSGEGAIADDAGNVSRNPALITMFDRPTFSAGAVYIDPDVNISGTSPSGRSLKADNIAPTAWVPNMHFVAPINDQFGWGASITSNYGLATEFNDTYAGGSVGGTTDLETMNLNLSGAYRLNNAWSFGLGFNAVYARAKIERFAGDLGQLVAGQIMQSPAGKTPQGQALAATANGIDSNTKIAHLNGNQWGFGWNAGILYELDKNNRYALTYRSEVKIDFKGNYSSDLNRVFNNYGLPIPTATGGATQSGYLTLNLPEMWEVSGYNRVDPQWAIHYSLAYTSWSQFQQLKATSTSGDTLFQKHEGFKDAYRIALGTTYYYDDNWTFRTGIAFDDSPVPAQNRSISIPDQDRFWLSAGTTYAFNKDASVDVGVSYMHGQSVKINEGPYQFESEGKAWLFGTNFNYAF
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Molecular Weight
61.9 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
The research on fadL recombinant protein primarily stems from its significant role in lipid metabolism and transport in various microorganisms. FadL, a member of the outer membrane protein family, is predominantly found in Gram-negative bacteria and functions as a long-chain fatty acid transporter. Understanding the structure and mechanism of fadL is crucial for elucidating its involvement in bacterial growth, adaptation, and pathogenicity. Furthermore, fadL's ability to facilitate the uptake of fatty acids can impact microbial biofilm formation and persistence in hostile environments, thus influencing microbial ecology and biotechnology applications. Studies have shown that the recombinant expression of fadL can lead to enhanced fatty acid uptake, making it a potential target for developing novel antimicrobial strategies or biotechnological processes to optimize lipid production in industrial microbiology. This research is also pivotal for exploring xeno-biosynthetic pathways and developing bioremediation techniques. Overall, the investigation into fadL and its recombinant protein is essential for advancing both fundamental microbiological knowledge and practical applications in healthcare and environmental science.
