Cat: IPD-X41627

Recombinant Escherichia coli cheA Protein ,His & Myc

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Analytical Data

  • Gene name

    cheA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Escherichia coli

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P07363

  • Expression Region

    1-654aa

  • Molecular Weight

    78.8 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.

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Protein Description

CheA is a histidine kinase that plays a crucial role in bacterial chemotaxis, which is the movement of bacteria toward or away from chemical stimuli. It serves as a key component of the chemotactic signaling pathway, acting as a sensory protein that undergoes autophosphorylation in response to environmental signals. This process initiates a cascade of events that ultimately influences bacterial movement. The study of CheA recombinant proteins has gained significance due to their potential applications in understanding bacterial behavior and signaling mechanisms. By producing and purifying recombinant CheA, researchers aim to elucidate its structure-function relationships, interactions with other signaling proteins, and the regulatory mechanisms governing its activity. Understanding these processes is essential not only for basic microbiology but also for the development of novel antimicrobial strategies, as manipulating the chemotactic response in bacteria could provide new ways to control bacterial behavior. Furthermore, the study of CheA and its associated proteins has implications in synthetic biology, where engineering bacterial sensors for environmental monitoring or therapeutic applications is of growing interest. Overall, the exploration of CheA at the molecular level contributes to a broader understanding of bacterial physiology and the intricate signaling networks that underpin their adaptive responses.

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