Cat: IPD-X41287

Recombinant Staphylococcus aureus pbp Protein ,His & Myc

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Analytical Data

  • Gene name

    pbp

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Staphylococcus aureus

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P07944

  • Expression Region

    344-670aa

  • Molecular Weight

    44.2 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.

Quality inspection process

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Protein Description

PBP (Penicillin-Binding Protein) recombinant proteins are critical in the study of bacterial cell wall biosynthesis and antibiotic resistance. These proteins play a vital role in the synthesis of peptidoglycan, a key component of bacterial cell walls, which is essential for maintaining the structural integrity of the cell. The increasing emergence of antibiotic-resistant bacterial strains, such as MRSA (Methicillin-resistant Staphylococcus aureus), has heightened the need for in-depth research into PBPs due to their target role in antibiotic action. Recombinant technology enables the production of PBP proteins in a controlled laboratory setting, allowing researchers to study their structure, function, and interactions with antibiotics like beta-lactams. Understanding the mechanisms by which PBPs confer resistance and how they can be targeted by novel therapeutics is crucial for developing new strategies to combat bacterial infections. Through the elucidation of PBP structures and functions, scientists aim to discover innovative inhibitors that can overcome resistance, providing a pathway for new antibiotic development and improving treatment outcomes for bacterial infections. The study of PBP recombinant proteins thus holds significant promise in addressing the challenges posed by antibiotic resistance in contemporary medicine.

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