Analytical Data
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Gene name
DEFb119
- Application
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Alternative Names
DEFB120; DEFB-19; DEFB-20
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8N690
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Expression Region
Lys22~Pro84
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Molecular Weight
40kDa
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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
DEFb119 is a defensin protein primarily found in amphibians, known for its antimicrobial properties and its role in the innate immune response. Defensins are small, cationic peptides that serve as crucial components of the immune system, functioning by disrupting microbial membranes and inactivating a range of pathogens, including bacteria, fungi, and viruses. As researchers continue to explore the potential therapeutic applications of antimicrobial peptides, DEFb119 has emerged as a subject of interest due to its unique structural features and efficacy against various drug-resistant organisms. Studies have demonstrated that DEFb119 exhibits not only strong antimicrobial activity but also promotes wound healing and shows potential in cancer treatment due to its cytotoxic properties against certain tumor cells. Understanding the mechanisms underlying DEFb119's action and stability can reveal new avenues for developing novel antimicrobial agents or adjuvants, contributing to the fight against increasing antibiotic resistance. Additionally, the comparative analysis of DEFb119 with other defensins might provide insights into the evolution of immune responses in vertebrates. The investigation into DEFb119 and similar peptides remains essential for harnessing their full potential in biomedical applications while advancing our overall knowledge of immune defense mechanisms in amphibians.
