Cat: IPD-X41755

Recombinant Streptococcus mitis comC Protein ,His & KSI

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Analytical Data

  • Gene name

    comC

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (CSP)

  • Species

    Streptococcus mitis

  • Source

    E. coli

  • Tag

    N- His-KSI

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O33666

  • Expression Region

    25-40aa

  • Molecular Weight

    17.3 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

The research on comC recombinant protein is rooted in the need to better understand the mechanisms of bacterial communication and its implications for pathogenesis. ComC, a key component of the competence signaling system in certain bacterial species, particularly in Streptococcus pneumoniae, plays a vital role in facilitating genetic transformation and intercellular communication. This protein is central to the competence pathway, where it acts as a signaling molecule that activates the expression of genes essential for DNA uptake and incorporation. Understanding the structure and function of comC is crucial for unraveling how bacteria coordinate group behavior and respond to environmental changes. Moreover, insights gained from studying comC could lead to novel therapeutic strategies targeting bacterial communication pathways, potentially mitigating issues like antibiotic resistance. As researchers employ techniques such as recombinant DNA technology and protein engineering, the exploration of comC promises to enhance our understanding of microbial dynamics in both health and disease contexts.

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