Cat: IPD-X40766

Recombinant Porphyromonas gingivalis PG_1424 Protein ,His

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Analytical Data

  • Gene name

    PG_1424

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    PG_1424Peptidylarginine deiminase; EC 3.5.3.-

  • Species

    Porphyromonas gingivalis

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9RQJ2

  • Expression Region

    44-556aa

  • Molecular Weight

    60.9 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

PG_1424 is a recombinant protein derived from the pathogen *Pseudomonas aeruginosa*, a bacterium known for its role in chronic infections, particularly in cystic fibrosis and immunocompromised patients. The study of PG_1424 arises from the need to understand the mechanisms of virulence and pathogenicity of this organism, as well as to develop potential therapeutic targets. Research has indicated that PG_1424 may play a critical role in the bacterium's ability to adapt and survive in hostile environments, contributing to its persistence in infected tissues. Investigating the structure and function of PG_1424 can provide insights into its interactions with host immune responses and its participation in biofilm formation, a significant factor in the chronicity of *Pseudomonas aeruginosa* infections. Furthermore, the recombinant expression of PG_1424 facilitates the production of large quantities of the protein, enabling advanced studies including crystallography, functional assays, and potential vaccine development. Understanding PG_1424's role could also pave the way for novel therapeutic strategies, potentially enhancing the efficacy of existing treatments against infections caused by *Pseudomonas aeruginosa*.

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