Cat: IPD-X26924

Recombinant Human ACSL1 Protein,His

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Analytical Data

  • Gene name

    ACSL1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ACS1; FACL1; FACL2; LACS; LACS1; LACS2; Fatty-Acid-Coenzyme A Ligase,Long-Chain 2; Lignoceroyl-CoA Synthase; Long-Chain Fatty-Acid-Coenzyme A Ligase 1

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P33121

  • Expression Region

    Gly457~Val698

  • Molecular Weight

    31kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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.

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Protein Description

ACSL1 (Acyl-CoA Synthetase Long-Chain Family Member 1) is an essential enzyme that plays a pivotal role in lipid metabolism by catalyzing the conversion of long-chain fatty acids into acyl-CoA, which is crucial for various cellular processes, including energy production, membrane synthesis, and signaling pathways. Dysfunction in ACSL1 has been implicated in several metabolic disorders, including obesity, diabetes, and cardiovascular diseases. Its significance in these conditions has spurred extensive research into its structure, function, and mechanisms of regulation. Recombinant ACSL1 protein has been generated to facilitate in-depth studies on its enzymatic activity, substrate specificity, and interactions with other metabolic pathways. Understanding the biochemical properties of ACSL1 through recombinant protein studies not only sheds light on its physiological role but also opens new avenues for therapeutic interventions targeting metabolic dysregulation. This area of research holds promise for developing innovative strategies to combat metabolic diseases where ACSL1's function is compromised, highlighting the importance of elucidating the intricate mechanisms governing fatty acid metabolism in health and disease.

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