Cat: IPD-X26068

Recombinant Human PDZD11 Protein,His & SUMO

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Analytical Data

  • Gene name

    PDZD11

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ATPase-interacting PDZ protein;Plasma membrane calcium ATPase-interacting single-PDZ protein ;PMCA-interacting single-PDZ protein

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q5EBL8

  • Expression Region

    1-140aa

  • Molecular Weight

    32.1 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

PGLYRP4, also known as PGRP-Iβ (Peptidoglycan Recognition Protein 4), is a member of the PGRP family, which plays a crucial role in the innate immune response by recognizing peptidoglycans from bacterial cell walls. The study of PGLYRP4 is significant due to its potential implications in host defense against bacterial infections and its involvement in the modulation of inflammatory responses. Research has shown that PGLYRP4 can enhance antibacterial activity by binding to bacterial peptidoglycans, thereby activating several immune pathways. Moreover, this protein has been implicated in various physiological processes beyond immune defense, including wound healing and tissue remodeling. The recombinant production of PGLYRP4 offers opportunities to explore its structural characteristics, functional roles, and interactions with bacterial pathogens in greater detail. Understanding the mechanisms by which PGLYRP4 operates could lead to novel therapeutic strategies for combating bacterial infections and managing inflammatory diseases. Given the rising concern over antibiotic resistance, studies focused on PGLYRP4 not only advance our basic understanding of immune regulation but also open avenues for the development of alternative antimicrobial agents. Thus, research into PGLYRP4/PGRP-Iβ recombinant protein is crucial, as it holds promise for both fundamental immunology and potential clinical applications in improving human health outcomes.

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