Analytical Data
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Gene name
DEFa2
- Application
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Alternative Names
DEFa2；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
37.2kDa
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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
DEFa2, a member of the defensin family, plays a vital role in the innate immune response. Defensins are small cationic peptides that exhibit antimicrobial activity against a broad range of pathogens, including bacteria, fungi, and viruses. Research into DEFa2 has gained momentum due to its potential therapeutic applications and its role in host defense mechanisms. Emerging studies have shown that DEFa2 possesses not only direct antimicrobial properties but also regulatory functions in immune modulation, influencing processes such as inflammation and wound healing. Understanding the structural characteristics and functional mechanisms of DEFa2 is crucial for developing novel antimicrobial agents, particularly in the face of rising antibiotic resistance. Moreover, DEFa2's involvement in various physiological and pathological processes highlights its significance in health and disease. As a recombinant protein, DEFa2 can be engineered and produced for detailed biochemical and biophysical studies, paving the way for its application in drug development and therapeutic interventions. Overall, the ongoing research on DEFa2 not only enhances our knowledge of host-pathogen interactions but also opens new avenues for innovative treatments targeting infectious diseases.
