Analytical Data
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Gene name
DEFb119
- Application
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Alternative Names
DEFb119；DEFB120；DEFB19；DEFB20；Beta-defensin 119
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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
Q8N690
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Expression Region
22-84aa
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AA Sequence
KRHILRCMG NSGICRASCK KNEQPYLYCR NCQSCCLQSY MRISISGKEE NTDWSYEKQW PRLP
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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
The DEFb119 recombinant protein has garnered significant attention in recent years due to its potential roles in immune response and antimicrobial activity. Originally identified from the skin secretion of amphibians, DEFb119 belongs to the family of defensins, which are small, cationic peptides known for their ability to disrupt microbial membranes. Research has suggested that defensins contribute to the innate immune system by exhibiting broad-spectrum activity against bacteria, fungi, and viruses. Moreover, the study of DEFb119 is particularly relevant in the context of increasing antibiotic resistance, as its unique mechanisms of action may provide alternative avenues for therapeutic development. In addition to its antimicrobial properties, DEFb119 has been implicated in modulating various cellular processes, including wound healing and inflammation. Consequently, understanding the structural and functional characteristics of DEFb119 could pave the way for innovative treatments and applications in both human health and veterinary medicine. Continued research into this recombinant protein could yield important insights into designing novel antimicrobial agents and enhancing our understanding of innate immune mechanisms.
