Analytical Data
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Gene name
DEFa3
- Application
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Alternative Names
DEFa3；DEF3；Neutrophil defensin 3
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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
P59666
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Expression Region
39-94aa
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AA Sequence
DIPEVVVSLAWDESLAPKHPGSRKNMDCYCRIPACIAGERRYGTCIYQGRLWAFCC
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Molecular Weight
8.4 kDa
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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
Related Products
Protein Description
DEFa3, belonging to the defensin family, is a small cationic peptide recognized for its antimicrobial properties and roles in the immune system. Initially identified in various species, including mammals, DEFa3 has garnered attention due to its potential therapeutic applications, particularly in combating infections and enhancing wound healing. The research on DEFa3 has expanded significantly in recent years, focusing on its structure-function relationship, mechanisms of action, and interaction with pathogens. Studies have shown that DEFa3 exhibits broad-spectrum antimicrobial activity, effective against bacteria, fungi, and viruses, making it a candidate for developing novel antimicrobial agents in the face of rising antibiotic resistance. Additionally, its ability to modulate immune responses suggests potential applications in treating inflammatory diseases and promoting tissue regeneration. As researchers delve deeper into the biochemical pathways influenced by DEFa3, the protein's role in innate immunity and its potential for clinical applications continue to be elucidated, paving the way for innovative therapeutic strategies.
