Analytical Data
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Gene name
DEFa1B
- Application
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Alternative Names
DEFa1B；DEF1；DEFA2；MRS；Neutrophil defensin 1
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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
P59665
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Expression Region
1-94aa
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AA Sequence
MRTLAILAAILLVALQAQAEPLQARADEVAAAPEQIAADIPEVVVSLAWDESLAPKHPGSRKNMACYCRIPACIAGERRYGTCIYQGRLWAFCC
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Molecular Weight
37.2 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
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Protein Description
DEFa1B, a member of the defensin family, is a small cationic peptide known for its antimicrobial properties and role in the immune response. Research on DEFa1B has gained significant interest due to its potential applications in therapeutic settings, particularly for its ability to combat various pathogens and its involvement in inflammation and host defense mechanisms. As a defensin, DEFa1B is characterized by its unique structural features, which include a compact fold stabilized by disulfide bonds, allowing it to interact effectively with microbial membranes. Studies have indicated that DEFa1B exhibits broad-spectrum antimicrobial activity, making it a promising candidate for drug development, especially amidst rising antibiotic resistance. Furthermore, understanding the mechanism of action of DEFa1B could lead to the design of novel peptide-based therapeutics. Investigations focus not only on its antimicrobial functions but also on how it modulates the immune response, which could have implications for autoimmune diseases and cancer therapy. The recombinant expression of DEFa1B has facilitated advanced studies and has opened up avenues for engineering variants with enhanced properties. Overall, the research surrounding DEFa1B is pivotal as it bridges microbiology, immunology, and pharmacology, aiming to leverage natural peptides for innovative health solutions.
