Analytical Data
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Gene name
DEFb112
- Application
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Alternative Names
DEFb112；DEFB12；Beta-defensin 112
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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
Q30KQ8
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Expression Region
1-113aa
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AA Sequence
MKLLTTICRLKLEKMYSKTNTSSTIFEKARHGTEKISTARSEGHHITFSRWKSCTAIGGRCKNQCDDSEFRISYCARPTTHCCVTECDPTDPNNWIPKDSVGTQEWYPKDSRH
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Molecular Weight
12.9 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
DEFb112 is a recombinant protein that has garnered attention in recent years due to its potential role in the field of immunology and therapeutic development. Originally identified from the defense response of amphibians, particularly the skin secretions of the Xenopus laevis frog, DEFb112 belongs to a family of antimicrobial peptides that exhibit bioactivity against a wide range of pathogens, including bacteria, fungi, and viruses. The increasing prevalence of antibiotic resistance has fueled the search for novel antimicrobial agents, making DEFb112 a focus of research for its unique mechanism of action and ability to modulate immune responses. Studies have demonstrated that DEFb112 not only possesses direct antimicrobial properties but also plays a role in promoting wound healing and modulating inflammation, thus making it a potential candidate for drug development in treating infections and inflammatory conditions. The recombinant expression of DEFb112 in various systems, such as E. coli and yeast, allows for the production of the peptide in a controlled manner for further characterization and evaluation of its therapeutic applications. Ongoing research aims to elucidate the structure-function relationship of DEFb112, optimize its formulation for clinical use, and evaluate its efficacy in preclinical models. The advancement in understanding of DEFb112's properties could lead to innovative strategies in combatting infectious diseases and enhancing immune responses, positioning it as a promising candidate in the realm of modern medicine.
