Analytical Data
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Gene name
Defb14
- Application
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Alternative Names
Defb14；DEFB14；Beta-defensin 114
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Species
Mouse
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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
Q7TNV9
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Expression Region
23-67aa
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AA Sequence
FLPKTLRKFFCRIRGGRCAVLNCLGKEEQIGRCSNSGRKCCRKKK
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Molecular Weight
21.2 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
Related Products
Protein Description
Defb14 is a member of the beta-defensin family, which consists of small cationic peptides known for their role in the innate immune response. Research on Defb14 has gained attention due to its antimicrobial properties, particularly against a variety of pathogens, including bacteria and fungi. Discovered primarily in human and mouse tissues, Defb14 is believed to be crucial in the first line of defense, acting by disrupting microbial cell membranes and modulating inflammatory responses. Studies have suggested that Defb14 also plays a role in wound healing and tissue repair, enhancing its significance in both health and disease contexts. Its expression can be influenced by several factors, such as infections, cytokines, and environmental stimuli, making it a target of interest in understanding host-pathogen interactions and immune system regulation. The potential therapeutic applications of Defb14 in treating infections and improving immune responses have propelled ongoing research, focusing on its biochemical properties, structural analysis, and mechanisms of action. By utilizing recombinant protein technology, researchers are investigating the functional characteristics of Defb14, which could lead to the development of novel antimicrobial peptides with clinical relevance. Overall, studying Defb14 and its recombinant forms could provide valuable insights into enhancing immune response and developing new strategies to combat antibiotic-resistant infections.
