Cat: IPD-X41495

Recombinant Streptococcus pneumoniae pbpX Protein ,Avi & His

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Analytical Data

  • Gene name

    pbpX

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (PBP-2X)(PBP2X)

  • Species

    Streptococcus pneumoniae

  • Source

    E. coli

  • Tag

    N- MBP & C- His-Avi

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P59676

  • Expression Region

    287-611aa

  • Molecular Weight

    83.2 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

PBPX, or Penicillin-Binding Protein X, is an important component of bacterial cell wall synthesis, particularly in certain pathogenic bacteria. Research into PBPX is driven by its critical role in antibiotic resistance, as it is involved in the formation of peptidoglycan, a vital structural component of bacterial cell walls. Given the increasing prevalence of antibiotic-resistant infections, understanding the structure and function of PBPX is essential for developing new therapeutic strategies. The recombinant production of PBPX allows for detailed biochemical studies and structural analyses that can elucidate its mechanisms and interactions with other cellular components. By investigating the properties of this protein, researchers aim to identify potential inhibitors that could serve as novel antibiotics or adjuvants in combination therapies. Furthermore, the study of PBPX can shed light on the evolutionary adaptations of bacteria to evade traditional antibiotic treatments, emphasizing the need for continuous research in this field to combat emerging health threats. Understanding PBPX and its role in antibiotic resistance could pave the way for innovative solutions to address the global challenge of drug-resistant infections.

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