Analytical Data
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Gene name
DEFb126
- Application
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Alternative Names
DEFb126；C20orf8；DEFB26；Beta-defensin 126
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BYW3
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Expression Region
21-63aa
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AA Sequence
NWYVKKCLND VGICKKKCKP EEMHVKNGWA MCGKQRDCCV PAD
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
The DEFb126 protein is part of the defensin family, which plays a critical role in the innate immune system of various organisms. Defensins are small, cysteine-rich cationic peptides that exhibit broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. The study of DEFb126, specifically identified in certain amphibian species, has garnered attention due to its unique functional properties and potential applications in biomedical research and therapeutic development. Researchers are particularly interested in understanding the mechanism of action of DEFb126 and its interaction with microbial membranes, as this could lead to the development of new antimicrobial agents that circumvent resistance mechanisms present in pathogenic microorganisms. Additionally, the structural analysis of DEFb126 can provide insights into the evolutionary adaptations of amphibian defensins, contributing to the broader field of host defense peptides. The exploration of DEFb126 not only enhances our knowledge of amphibian immunology but also holds promise for innovative approaches to combat infections in human medicine. Through recombinant expression and characterization of DEFb126, scientists aim to determine its stability, bioactivity, and potential synergistic effects with existing antibiotics, creating avenues for novel therapeutic strategies in the face of rising antibiotic resistance.
