Cat: PA2000-2625

Recombinant E.coli yjbL Protein,His

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Analytical Data

  • Gene name

    yjbL

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    yjbL;UPF0738 Protein YjbL

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P32693

  • Expression Region

    1-84aa

  • AA Sequence

    MLKIIPGATGYFNKTLNSNQFDNEDAIKDKLDNRGSIKGKLNNIYGKSIDYAALRHRDIIIAKIDLFIQRITHNLWHARKKMCF

  • Molecular Weight

    25.1 kDa

  • 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.

Quality inspection process

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Protein Description

YjbL is a protein found in various bacterial species, and it has garnered attention in recent years due to its potential role in microbial physiology and metabolism. Research into YjbL has been driven by its association with stress responses and its involvement in cellular processes, such as biofilm formation and antibiotic resistance. Understanding the function of YjbL is crucial, as it may contribute to bacterial adaptation in hostile environments and influence pathogenicity. Furthermore, studying YjbL can provide insights into the molecular mechanisms underlying bacterial survival strategies, which are critical for developing new antimicrobial therapies. Investigations into the structural and functional aspects of YjbL, including its interactions with other cellular components, are ongoing. These studies aim to elucidate how YjbL contributes to the overall fitness of microorganisms and its potential applicability in biotechnology and medicine. As researchers continue to explore YjbL's biochemical properties and regulatory networks, there is hope that this protein could serve as a target for innovative approaches in combating bacterial infections.

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