Cat: PA2000-1021

Recombinant Human PEG Protein,His

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Analytical Data

  • Gene name

    PEG

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    PEG;KIAA0287;ZSCAN24;Paternally-expressed gene 3 Protein

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P09466

  • Expression Region

    19-180aa

  • AA Sequence

    MDIPQTKQDLELPKLAGTWHSMAMATNNISLMATLKAPLRVHITSLLPTPEDNLEIVLHRWENNSCVEKKVLGEKTENPKKFKINYTVANEATLLDTDYDNFLFLCLQDTTTPIQSMMCQYLARVLVEDDEIMQGFIRAFRPLPRHLWYLLDLKQMEEPCRF

  • Molecular Weight

    24.8 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.

Quality inspection process

Related Products

Protein Description

PEGylated recombinant proteins have emerged as a significant advancement in biotechnology and therapeutic development, reflecting a convergence of protein engineering and polymer chemistry. The foundational concept behind PEGylation—the process of attaching polyethylene glycol (PEG) molecules to proteins—addresses several pivotal challenges in pharmaceutical protein therapies, including stability, solubility, and bioavailability. As recombinant proteins have gained prominence in treating various diseases, including cancers and genetic disorders, their innate properties often limit their clinical efficacy due to rapid clearance and immunogenicity. By modifying the surface characteristics of these proteins through PEGylation, researchers aim to prolong their circulation time in the bloodstream, enhance their therapeutic index, and reduce adverse immune reactions. This modification fosters a more favorable pharmacokinetic profile, leading to improved dosage regimens and patient compliance. The journey of PEGylated proteins has seen significant milestones, from initial proofs of concept to successful marketable drugs such as pegfilgrastim and peginterferon. Consequently, ongoing research continues to explore the optimal conditions for PEGylation, including the choice of PEG size and structure, as well as the specific attachment sites on the protein backbone, thereby tailoring their properties for diverse applications. Overall, PEGylated recombinant proteins represent a dynamic and evolving field, integrating multifaceted research efforts to revolutionize therapeutics and enhance patient care.

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