Cat: IPD-X29233

Recombinant Bovine Cathelicidin-4 Protein,His & SUMO

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Analytical Data

  • Gene name

    Cathelicidin-4

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Indolicidin

  • Species

    Bovine

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P33046

  • Expression Region

    131-143aa

  • Molecular Weight

    17.9 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.

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Protein Description

Cathelicidin-4 (CATH-4) is a member of the cathelicidin family of antimicrobial peptides, which play a crucial role in the innate immune response of various organisms. Initially discovered in specific vertebrates, such as humans and mice, CATH-4 is known for its potent antimicrobial properties against a wide range of pathogens, including bacteria, viruses, and fungi. Its mechanism of action involves disrupting microbial membranes, leading to cell lysis. Research into CATH-4 is particularly relevant due to the increasing prevalence of antibiotic-resistant infections, making the development of new antimicrobial agents imperative. Furthermore, CATH-4 exhibits additional functions, including immunomodulatory effects, promoting wound healing and modulating inflammatory responses. Studies have shown that this peptide can enhance the activity of other immune cells, thus contributing to a more comprehensive approach to infection control. Additionally, recombinant technology has enabled the production of CATH-4 in vitro, facilitating detailed studies on its structure-function relationship and therapeutic potential. Investigating CATH-4 not only contributes to the fundamental understanding of innate immunity but also opens avenues for the development of novel therapeutics in combating resistant microbial strains and improving clinical outcomes in infectious diseases. As such, CATH-4 represents a promising candidate in the search for effective antimicrobial therapies and serves as a critical focus for further research in immunology and infectious disease management.

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