Cat: IPD-X40100

Recombinant Mouse Defb4 Protein ,His & SUMO

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Analytical Data

  • Gene name

    Defb4

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Defensin, beta 4

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P82019

  • Expression Region

    23-63aa

  • Molecular Weight

    20.6 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

Defb4, also known as antimicrobial peptide Defensin beta 4, is a crucial component of the innate immune system, primarily expressed in epithelial tissues such as the skin and mucosal surfaces. Its primary function is to provide a first line of defense against microbial infections by exhibiting broad-spectrum antimicrobial properties, including antibacterial, antifungal, and antiviral activities. Research interest in Defb4 has surged due to its potential therapeutic applications, particularly in the context of increasing antibiotic resistance and rising infectious diseases. The peptide works by disrupting microbial membranes and modulating host immune responses, suggesting its role not only as a direct antimicrobial agent but also as an immunomodulator. Recent studies have focused on the recombination and production of Defb4 in various expression systems, which allows for detailed structural and functional analysis. Understanding its mechanisms can pave the way for the development of novel antimicrobial drugs and enhance current therapies against pathogens that have developed resistance to conventional antibiotics. Moreover, exploring the genetic regulation of Defb4 expression can provide insights into its role in diseases characterized by dysregulated immune responses, such as chronic inflammation and cancer. Overall, the study of recombinant Defb4 represents a promising frontier in both basic research and clinical applications, highlighting the need for continued exploration of its potential as a versatile therapeutic agent in modern medicine.

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